{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,12]],"date-time":"2026-08-12T15:10:30Z","timestamp":1786547430603,"version":"build-2736575974"},"reference-count":66,"publisher":"American Chemical Society (ACS)","issue":"31","license":[{"start":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T00:00:00Z","timestamp":1785110400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T00:00:00Z","timestamp":1785110400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T00:00:00Z","timestamp":1785110400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM148766"],"award-info":[{"award-number":["GM148766"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI185198"],"award-info":[{"award-number":["AI185198"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,8,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Many transmembrane (TM) proteins contain an amphipathic helix. These amphipathic helices can sense lipid composition, stabilize membrane curvature, and mediate protein\u2013protein interactions. Here, we combined solid-state NMR spectroscopy (ssNMR) and molecular dynamics simulations to characterize the structure and membrane interactions of a minimal TM and amphipathic construct (residues 101\u2013146) from Mycobacterium tuberculosis (Mtb) FtsL. Amino-acid-specific 15N-labeled oriented-sample ssNMR spectra in POPC\/POPG (4:1 molar ratio) membranes uniquely defined the orientation of the TM helix (residues 124\u2013144), including a 16\u00b0 tilt, but constrained only the amphipathic helix (residues 101\u2013114) to a 90\u00b0 tilt, leaving ambiguity in helical rotation and membrane burial depth. To resolve this ambiguity, we determined the two-dimensional free-energy surface using umbrella sampling simulations. The free-energy surface featured a major bound minimum, with the side chains of Leu104, Leu107, and Ile111 projecting into the hydrophobic core of the membrane and those of Arg103, Arg107, and Arg114 projecting sideways to interact with lipid headgroups. In pure POPC membranes, the bound basin contracted while the unbound basin expanded, as electrostatic attraction between Arg side chains and acidic POPG was replaced with repulsion by POPC\u2019s choline group. The final structure of FtsL101\u2013146 was refined by restrained molecular dynamics simulations in a POPC\/POPG bilayer and further validated by 13C\u201313C correlation magic-angle-spinning NMR. Together, these results demonstrate that the amphipathic helix of FtsL functions as a membrane-interacting element that stabilizes the protein in the membrane environment and mediates the recruitment of downstream proteins to the divisome for Mtb cell division.<\/jats:p>","DOI":"10.1021\/jacs.6c12502","type":"journal-article","created":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T13:10:38Z","timestamp":1785849038000},"page":"33990-34001","source":"Crossref","is-referenced-by-count":0,"title":["Structure and Membrane\nInteractions of Two Helices\nfrom\n                    <i>Mycobacterium tuberculosis<\/i>\n                    FtsL,\nOne Transmembrane and One Amphipathic"],"prefix":"10.1021","volume":"148","author":[{"given":"Jiaxing","family":"Fan","sequence":"first","affiliation":[{"name":"Florida State University , , , ,","place":["Tallahassee, Florida, United States, 32306"]},{"name":"National High Magnetic Field Laboratory , , , ,","place":["Tallahassee, Florida, United States, 32310"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9184-779X","authenticated-orcid":true,"given":"Ramesh","family":"Prasad","sequence":"additional","affiliation":[{"name":"University of Illinois Chicago , , , ,","place":["Chicago, Illinois, United States, 60607"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rongfu","family":"Zhang","sequence":"additional","affiliation":[{"name":"Florida State University , , , ,","place":["Tallahassee, Florida, United States, 32306"]},{"name":"National High Magnetic Field Laboratory , , , ,","place":["Tallahassee, Florida, United States, 32310"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wenhao","family":"Hu","sequence":"additional","affiliation":[{"name":"Florida State University , , , ,","place":["Tallahassee, Florida, United States, 32306"]},{"name":"National High Magnetic Field Laboratory , , , ,","place":["Tallahassee, Florida, United States, 32310"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9413-0505","authenticated-orcid":true,"given":"Timothy A.","family":"Cross","sequence":"additional","affiliation":[{"name":"Florida State University , , , ,","place":["Tallahassee, Florida, United States, 32306"]},{"name":"National High Magnetic Field Laboratory , , , ,","place":["Tallahassee, Florida, United States, 32310"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9020-0302","authenticated-orcid":true,"given":"Huan-Xiang","family":"Zhou","sequence":"additional","affiliation":[{"name":"University of Illinois Chicago , , , ,","place":["Chicago, Illinois, United States, 60607"]},{"name":"University of Illinois Chicago , , , ,","place":["Chicago, Illinois, United States, 60607"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0677-5897","authenticated-orcid":true,"given":"Yan-Yan","family":"Hu","sequence":"additional","affiliation":[{"name":"Florida State University , , , ,","place":["Tallahassee, Florida, United States, 32306"]},{"name":"National High Magnetic Field Laboratory , , , ,","place":["Tallahassee, Florida, United States, 32310"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,7,27]]},"reference":[{"key":"2026081210084455600_cit1","unstructured":"World Health Organization.\n          . 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Immunopathol."},{"issue":"3","key":"2026081210084455600_cit5","doi-asserted-by":"publisher","DOI":"10.3390\/tropicalmed7030048","article-title":"The Biological and\nClinical Aspects of a Latent Tuberculosis Infection","volume":"7","author":"Khabibullina","year":"2022","journal-title":"Trop. Med. Infect. Dis."},{"issue":"2\u20133","key":"2026081210084455600_cit6","doi-asserted-by":"publisher","first-page":"202","DOI":"10.1007\/s12026-011-8229-7","article-title":"Latent Tuberculosis:\nWhat the Host \u201cSees\u201d?","volume":"50","author":"Gideon","year":"2011","journal-title":"Immunol.\nRes."},{"issue":"7656","key":"2026081210084455600_cit7","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1038\/NATURE22361","article-title":"Deletion of a Mycobacterial\nDivisome\nFactor Collapses Single-Cell Phenotypic Heterogeneity","volume":"546","author":"Rego","year":"2017","journal-title":"Nature"},{"key":"2026081210084455600_cit8","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.49570","article-title":"Persistent Mycobacterium Tuberculosis\nInfection in Mice Requires PerM for Successful Cell Division","volume":"8","author":"Wang","year":"2019","journal-title":"eLife"},{"key":"2026081210084455600_cit9","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2024.1415554","article-title":"Regulatory Role of\nMycobacterium Tuberculosis MtrA on Dormancy\/Resuscitation Revealed\nby a Novel Target Gene-Mining Strategy","volume":"15","author":"Fu","year":"2024","journal-title":"Front.\nMicrobiol."},{"issue":"2","key":"2026081210084455600_cit10","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1111\/mmi.13696","article-title":"Assembly and\nActivation of the Escherichia Coli Divisome","volume":"105","author":"Du","year":"2017","journal-title":"Mol. 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Chem."},{"issue":"6349","key":"2026081210084455600_cit13","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1038\/354161a0","article-title":"FtsZ Ring Structure Associated with Division in Escherichia Coli","volume":"354","author":"Bi","year":"1991","journal-title":"Nature"},{"issue":"1","key":"2026081210084455600_cit14","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1038\/s41579-023-00942-x","article-title":"Insights into\nthe Assembly and Regulation of the Bacterial\nDivisome","volume":"22","author":"Cameron","year":"2024","journal-title":"Nat. Rev. Microbiol."},{"issue":"5","key":"2026081210084455600_cit15","doi-asserted-by":"publisher","first-page":"1315","DOI":"10.1111\/j.1365-2958.2004.04044.x","article-title":"A Complex of the Escherichia Coli Cell Division Proteins FtsL, FtsB\nand FtsQ Forms Independently of\nIts Localization to the Septal Region","volume":"52","author":"Buddelmeijer","year":"2004","journal-title":"Mol.\nMicrobiol."},{"issue":"1","key":"2026081210084455600_cit16","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-37543-4","article-title":"Structure\nof the Heterotrimeric Membrane Protein Complex FtsB-FtsL-FtsQ of the\nBacterial Divisome","volume":"14","author":"Nguyen","year":"2023","journal-title":"Nat. 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Bacteriol."},{"issue":"1","key":"2026081210084455600_cit19","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1111\/j.1574-6968.2002.tb11409.x","article-title":"Topological Characterization of the Essential Escherichia Coli Cell Division Protein FtsW","volume":"216","author":"Lara","year":"2002","journal-title":"FEMS Microbiol. Lett."},{"issue":"6","key":"2026081210084455600_cit20","doi-asserted-by":"publisher","first-page":"1149","DOI":"10.1038\/s41564-023-01368-0","article-title":"Cryo-EM Structure\nof the Bacterial Divisome Core Complex\nand Antibiotic Target FtsWIQBL","volume":"8","author":"Ka\u0308shammer","year":"2023","journal-title":"Nat. Microbiol."},{"issue":"1","key":"2026081210084455600_cit21","doi-asserted-by":"publisher","DOI":"10.1038\/s41421-023-00629-w","article-title":"Structural Insights into the Activation\nof the Divisome Complex FtsWIQLB","volume":"10","author":"Yang","year":"2024","journal-title":"Cell Discovery"},{"issue":"6","key":"2026081210084455600_cit22","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.03012-20","article-title":"Essential\nRole for Ftsl in Activation of Septal Peptidoglycan\nSynthesis","volume":"11","author":"Park","year":"2020","journal-title":"mBio"},{"issue":"3","key":"2026081210084455600_cit23","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1080\/096876899294544","article-title":"Amphitropic Proteins: Regulation by Reversible Membrane\nInteractions (Review)","volume":"16","author":"Johnson","year":"1999","journal-title":"Mol. Membr. Biol."},{"issue":"1","key":"2026081210084455600_cit24","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1016\/j.jmb.2004.11.036","article-title":"A Study of the Membrane-Water Interface\nRegion of Membrane Proteins","volume":"346","author":"Granseth","year":"2005","journal-title":"J. Mol. Biol."},{"key":"2026081210084455600_cit25","doi-asserted-by":"crossref","unstructured":"Rombach, J.; Theiss, T.; Nielsen, E.; Schmidt, J. H.; Agenant, J.; Larsen, A. H.; Madsen, K. L.\n          A Proteome-Wide\nScreen for Membrane-Interactions in Intrinsically Disordered Regions\nof Transmembrane Proteins Reveals a Role in Disease\n          bioRxiv\n          2025\n          10.1101\/2025.08.15.670465.","DOI":"10.1101\/2025.08.15.670465"},{"issue":"7","key":"2026081210084455600_cit26","doi-asserted-by":"publisher","first-page":"E639","DOI":"10.1073\/PNAS.1415882112","article-title":"A Conserved Amphipathic\nHelix Is Required for Membrane Tubule Formation by Yop1p","volume":"112","author":"Brady","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"1","key":"2026081210084455600_cit27","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-021-85866-3","article-title":"Curvature Sensing Amphipathic Helix\nin the C-Terminus of RTNLB13 Is Conserved in All Endoplasmic Reticulum\nShaping Reticulons in Arabidopsis Thaliana","volume":"11","author":"Brooks","year":"2021","journal-title":"Sci. Rep."},{"issue":"5480","key":"2026081210084455600_cit28","doi-asserted-by":"publisher","first-page":"739","DOI":"10.1126\/SCIENCE.289.5480.739","article-title":"Crystal Structure\nof\nRhodopsin: A G Protein-Coupled Receptor","volume":"289","author":"Palczewski","year":"2000","journal-title":"Science"},{"issue":"2","key":"2026081210084455600_cit29","doi-asserted-by":"publisher","first-page":"118","DOI":"10.1016\/j.mce.2009.01.002","article-title":"Role of\nHelix 8 in G Protein-Coupled Receptors Based on Structure-Function\nStudies on the Type 1 Angiotensin Receptor","volume":"302","author":"Huynh","year":"2009","journal-title":"Mol. Cell. Endocrinol."},{"issue":"26","key":"2026081210084455600_cit30","doi-asserted-by":"publisher","first-page":"8298","DOI":"10.1021\/bi025534m","article-title":"Evidence That Helix\n8 of Rhodopsin Acts as a Membrane-Dependent Conformational Switch","volume":"41","author":"Krishna","year":"2002","journal-title":"Biochemistry"},{"issue":"1","key":"2026081210084455600_cit31","doi-asserted-by":"publisher","DOI":"10.1038\/s42003-023-04686-5","article-title":"An Arg\/Ala-Rich\nHelix in the N-Terminal Region of M. Tuberculosis FtsQ Is a Potential\nMembrane Anchor of the Z-Ring","volume":"6","author":"Smrt","year":"2023","journal-title":"Commun. Biol."},{"issue":"8016","key":"2026081210084455600_cit32","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate Structure\nPrediction of\nBiomolecular Interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"issue":"1","key":"2026081210084455600_cit33","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1146\/annurev-biophys-083012-130326","article-title":"Influences of Membrane Mimetic Environments\non Membrane\nProtein Structures","volume":"42","author":"Zhou","year":"2013","journal-title":"Annu. Rev. Biophys."},{"issue":"10","key":"2026081210084455600_cit34","doi-asserted-by":"publisher","first-page":"1830","DOI":"10.1016\/j.str.2016.07.017","article-title":"From Nanodiscs to Isotropic Bicelles: A Procedure for\nSolution Nuclear Magnetic Resonance Studies of Detergent-Sensitive\nIntegral Membrane Proteins","volume":"24","author":"Laguerre","year":"2016","journal-title":"Structure"},{"issue":"6","key":"2026081210084455600_cit35","doi-asserted-by":"publisher","first-page":"4669","DOI":"10.1021\/acs.chemrev.6b00690","article-title":"Nanodiscs in Membrane Biochemistry and Biophysics","volume":"117","author":"Denisov","year":"2017","journal-title":"Chem. Rev."},{"issue":"11","key":"2026081210084455600_cit36","doi-asserted-by":"publisher","first-page":"2256","DOI":"10.1038\/nprot.2013.129","article-title":"Lipid Bilayer\nPreparations of Membrane\nProteins for Oriented and Magic-Angle Spinning Solid-State NMR Samples","volume":"8","author":"Das","year":"2013","journal-title":"Nat. Protoc."},{"issue":"39","key":"2026081210084455600_cit37","doi-asserted-by":"publisher","first-page":"30092","DOI":"10.1074\/jbc.M004658200","article-title":"Phosphatidylinositol\nIs an Essential\nPhospholipid of Mycobacteria","volume":"275","author":"Jackson","year":"2000","journal-title":"J. Biol. Chem."},{"issue":"6","key":"2026081210084455600_cit38","doi-asserted-by":"publisher","first-page":"2876","DOI":"10.1038\/nprot.2006.202","article-title":"Using Circular\nDichroism Spectra to Estimate Protein Secondary Structure","volume":"1","author":"Greenfield","year":"2006","journal-title":"Nat. Protoc."},{"issue":"18","key":"2026081210084455600_cit39","doi-asserted-by":"publisher","first-page":"4859","DOI":"10.1039\/C5CS00084J","article-title":"Circular Dichroism\nSpectroscopy of Membrane Proteins","volume":"45","author":"Miles","year":"2016","journal-title":"Chem. Soc.\nRev."},{"issue":"1","key":"2026081210084455600_cit40","doi-asserted-by":"publisher","first-page":"150","DOI":"10.1006\/jmre.2000.2035","article-title":"A Solid-State NMR Index of Helical Membrane Protein\nStructure and Topology","volume":"144","author":"Marassi","year":"2000","journal-title":"J. Magn. Reson."},{"issue":"1","key":"2026081210084455600_cit41","doi-asserted-by":"publisher","first-page":"162","DOI":"10.1006\/jmre.2000.2037","article-title":"Imaging Membrane\nProtein Helical Wheels","volume":"144","author":"Wang","year":"2000","journal-title":"J. Magn. Reson."},{"issue":"2","key":"2026081210084455600_cit42","doi-asserted-by":"publisher","first-page":"E119","DOI":"10.1073\/pnas.1415908112","article-title":"Structure\nof CrgA, a Cell Division Structural and Regulatory Protein from Mycobacterium\nTuberculosis, in Lipid Bilayers","volume":"112","author":"Das","year":"2015","journal-title":"Proc. Natl.\nAcad. Sci. U.S.A."},{"issue":"13","key":"2026081210084455600_cit43","doi-asserted-by":"publisher","first-page":"11117","DOI":"10.1021\/jacs.4c17168","article-title":"Mycobacterium Tuberculosis\nCrgA Forms a Dimeric Structure\nwith Its Transmembrane Domain Sandwiched between Cytoplasmic and Periplasmic\n\u03b2-Sheets, Enabling Multiple Interactions with Other Divisome\nProteins","volume":"147","author":"Shin","year":"2025","journal-title":"J. Am. Chem. Soc."},{"issue":"2\u20133","key":"2026081210084455600_cit44","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1016\/j.bpc.2010.11.002","article-title":"The Structural\nand Topological Analysis\nof Membrane-Associated Polypeptides by Oriented Solid-State NMR Spectroscopy:\nEstablished Concepts and Novel Developments","volume":"153","author":"Bechinger","year":"2011","journal-title":"Biophys. Chem."},{"issue":"1","key":"2026081210084455600_cit45","doi-asserted-by":"publisher","DOI":"10.1038\/s42003-023-05490-x","article-title":"Dimeric\nTransmembrane Structure of the SARS-CoV-2 E Protein","volume":"6","author":"Zhang","year":"2023","journal-title":"Commun. Biol."},{"issue":"2","key":"2026081210084455600_cit46","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1007\/s10858-013-9732-z","article-title":"Practical Use of Chemical\nShift Databases for Protein Solid-State NMR: 2D Chemical Shift Maps\nand Amino-Acid Assignment with Secondary-Structure Information","volume":"56","author":"Fritzsching","year":"2013","journal-title":"J. Biomol. 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