{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T01:42:50Z","timestamp":1790905370637,"version":"4.1.0"},"reference-count":49,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2009,7,20]],"date-time":"2009-07-20T00:00:00Z","timestamp":1248048000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2010,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:italic>Shigella dysentriae<\/jats:italic> and other Gram\u2010negative human pathogens are able to use iron from heme bound to hemoglobin for growing. We solved at 2.6 \u00c5 resolution the 3D structure of the TonB\u2010dependent heme\/hemoglobin outer membrane receptor ShuA from <jats:italic>S. dysenteriae<\/jats:italic>. ShuA binds to hemoglobin and transports heme across the outer membrane. The structure consists of a C\u2010terminal domain that folds into a 22\u2010stranded transmembrane \u03b2\u2010barrel, which is filled by the N\u2010terminal plug domain. One distal histidine ligand of heme is located at the apex of the plug, exposed to the solvent. His86 is situated 9.86 \u00c5 apart from His420, the second histidine involved in the heme binding. His420 is in the extracellular loop L7. The heme coordination by His86 and His420 involves conformational changes. The comparisons with the hemophore receptor HasR of <jats:italic>Serratia marcescens<\/jats:italic> bound to HasA\u2010Heme suggest an extracellular induced fit mechanism for the heme binding. The loop L7 contains hydrophobic residues which could interact with the hydrophobic porphyring ring of heme. The energy required for the transport by ShuA is derived from the proton motive force after interactions between the periplasmic N\u2010terminal TonB\u2010box of ShuA and the inner membrane protein, TonB. In ShuA, the TonB\u2010box is buried and cannot interact with TonB. The structural comparisons with HasR suggest its conformational change upon the heme binding for interacting with TonB. The signaling of the heme binding could involve a hydrogen bond network going from His86 to the TonB\u2010box. Proteins 2010. \u00a9 2009 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.22539","type":"journal-article","created":{"date-parts":[[2009,7,21]],"date-time":"2009-07-21T14:09:11Z","timestamp":1248185351000},"page":"286-294","source":"Crossref","is-referenced-by-count":51,"title":["Structure of the heme\/hemoglobin outer membrane receptor ShuA from <i>Shigella dysenteriae<\/i>: Heme binding by an induced fit mechanism"],"prefix":"10.1002","volume":"78","author":[{"given":"David","family":"Cobessi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahmed","family":"Meksem","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karl","family":"Brillet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,9,3]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.288.5471.1651"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.200318797"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0968-0004(99)01359-6"},{"key":"e_1_2_6_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2736(02)00578-3"},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2000.01987.x"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.68.1.154-171.2004"},{"key":"e_1_2_6_8_2","doi-asserted-by":"crossref","first-page":"5008","DOI":"10.1128\/iai.64.12.5008-5014.1996","article-title":"Identification and purification of a hemoglobin\u2010binding outer membrane protein from Neisseria gonorrhoeae","volume":"64","author":"Chen CJ","year":"1996","journal-title":"Infect Immun"},{"key":"e_1_2_6_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.70.10.5390-5403.2002"},{"key":"e_1_2_6_10_2","doi-asserted-by":"publisher","DOI":"10.1007\/s10534-006-9050-y"},{"key":"e_1_2_6_11_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0809406106"},{"key":"e_1_2_6_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0378-1097(03)00761-4"},{"key":"e_1_2_6_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2001.tb00569.x"},{"key":"e_1_2_6_14_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2672.2000.01031.x"},{"key":"e_1_2_6_15_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M611121200"},{"key":"e_1_2_6_16_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.65.12.5358-5363.1997"},{"key":"e_1_2_6_17_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444909002200"},{"key":"e_1_2_6_18_2","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1107\/S1744309109008148","article-title":"Expression, purification, crystallization and preliminary X\u2010ray diffraction analysis of the TonB\u2010dependent haem outer membrane transporter ShuA from Shigella dysenteriae","volume":"65","author":"Brillet K","year":"2009","journal-title":"Acta Crystallogr F"},{"key":"e_1_2_6_19_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889893005588"},{"key":"e_1_2_6_20_2","first-page":"64112","article-title":"A short history of SHELX","author":"Sheldrick GM","year":"2008","journal-title":"Acta Crystallogr A"},{"key":"e_1_2_6_21_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889804018047"},{"key":"e_1_2_6_22_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(97)76073-7"},{"key":"e_1_2_6_23_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444995008754"},{"key":"e_1_2_6_24_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444904019158"},{"key":"e_1_2_6_25_2","doi-asserted-by":"crossref","first-page":"2728","DOI":"10.1038\/nprot.2007.406","article-title":"Version 1.2 of the crystallography and NMR system","volume":"2","author":"Brunger AT","year":"2002","journal-title":"Nat Protoc"},{"key":"e_1_2_6_26_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444996012255"},{"key":"e_1_2_6_27_2","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","volume":"50","author":"CCP4","year":"1994","journal-title":"Acta Crystallogr D"},{"key":"e_1_2_6_28_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889892009944"},{"key":"e_1_2_6_29_2","volume-title":"The PyMOL molecular graphics system","author":"Delano WL","year":"2002"},{"key":"e_1_2_6_30_2","doi-asserted-by":"publisher","DOI":"10.1038\/355472a0"},{"key":"e_1_2_6_31_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444904026460"},{"key":"e_1_2_6_32_2","doi-asserted-by":"publisher","DOI":"10.1038\/4931"},{"key":"e_1_2_6_33_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2005.01.021"},{"key":"e_1_2_6_34_2","doi-asserted-by":"publisher","DOI":"10.1038\/nsb914"},{"key":"e_1_2_6_35_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(03)00855-6"},{"key":"e_1_2_6_36_2","doi-asserted-by":"publisher","DOI":"10.1007\/s10534-006-9060-9"},{"key":"e_1_2_6_37_2","doi-asserted-by":"crossref","first-page":"6063","DOI":"10.1128\/JB.181.19.6063-6072.1999","article-title":"Use of the heme\u2010protein complexes by the Yersina enterocolitica HemR receptor: histidine residues are essential for receptor function","volume":"181","author":"Bracken CS","year":"1999","journal-title":"J Bacteriol"},{"key":"e_1_2_6_38_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bb.21.060192.000453"},{"key":"e_1_2_6_39_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2005.08.004"},{"key":"e_1_2_6_40_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.emboj.7601693"},{"key":"e_1_2_6_41_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.186.11.3578-3589.2004"},{"key":"e_1_2_6_42_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1128057"},{"key":"e_1_2_6_43_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1127694"},{"key":"e_1_2_6_44_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi027120z"},{"key":"e_1_2_6_45_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.282.5397.2215"},{"key":"e_1_2_6_46_2","first-page":"771","article-title":"Transmembrane signaling across the ligand\u2010gated FhuA receptor: crystal structures of free and ferrichrome\u2010bound states reveal allosteric changes","volume":"95","author":"Locher KP","year":"1998","journal-title":"Science"},{"key":"e_1_2_6_47_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1067313"},{"key":"e_1_2_6_48_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2007.02.023"},{"key":"e_1_2_6_49_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1998.00873.x"},{"key":"e_1_2_6_50_2","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/15.4.305"}],"container-title":["Proteins: Structure, Function, and Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fprot.22539","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/prot.22539","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,15]],"date-time":"2023-10-15T13:04:28Z","timestamp":1697375068000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/prot.22539"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,9,3]]},"references-count":49,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2010,2]]}},"alternative-id":["10.1002\/prot.22539"],"URL":"https:\/\/doi.org\/10.1002\/prot.22539","archive":["Portico"],"relation":{},"ISSN":["0887-3585","1097-0134"],"issn-type":[{"value":"0887-3585","type":"print"},{"value":"1097-0134","type":"electronic"}],"subject":[],"published":{"date-parts":[[2009,9,3]]}}}