{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,18]],"date-time":"2026-05-18T12:01:59Z","timestamp":1779105719700,"version":"3.51.4"},"reference-count":44,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2022,1,10]],"date-time":"2022-01-10T00:00:00Z","timestamp":1641772800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31870836"],"award-info":[{"award-number":["31870836"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MedComm"],"published-print":{"date-parts":[[2022,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:italic>Listeria monocytogenes<\/jats:italic>, a food\u2010borne Gram\u2010positive pathogen, often causes diseases such as gastroenteritis, bacterial sepsis, and meningitis. Newly discovered extracellular electron transfer (EET) from <jats:italic>L. monocytogenes<\/jats:italic> plays critical roles in the generation of redox molecules as electron carriers in bacteria. A Mg<jats:sup>2+<\/jats:sup>\u2010dependent protein flavin mononucleotide (FMN) transferase (FmnB; UniProt: LMRG_02181) in EET is responsible for the transfer of electrons from intracellular to extracellular by hydrolyzing cofactor flavin adenine dinucleotide (FAD) and transferring FMN. FmnB homologs have been investigated in Gram\u2010negative bacteria but have been less well studied in Gram\u2010positive bacteria. In particular, the catalytic and inhibitory mechanisms of FmnB homologs remain elusive. Here, we report a series of crystal structures of apo\u2010FmnB and FmnB complexed with substrate FAD, three inhibitors AMP, ADP, and ATP, revealing the unusual catalytic triad center (Asp301\u2010Ser257\u2010His273) of FmnB. The three inhibitors indeed inhibited the activity of FmnB in varying degrees by occupying the binding site of the FAD substrate. The key residue Arg262 of FmnB was profoundly affected by ADP but not AMP or ATP. Overall, our studies not only provide insights into the promiscuous ligand recognition behavior of FmnB but also shed light on its catalytic and inhibitory mechanisms.<\/jats:p>","DOI":"10.1002\/mco2.99","type":"journal-article","created":{"date-parts":[[2022,1,10]],"date-time":"2022-01-10T14:54:44Z","timestamp":1641826484000},"source":"Crossref","is-referenced-by-count":2,"title":["Structural insights into the catalytic and inhibitory mechanisms of the flavin transferase FmnB in <i>Listeria monocytogenes<\/i>"],"prefix":"10.1002","volume":"3","author":[{"given":"Yanhui","family":"Zheng","sequence":"first","affiliation":[{"name":"Division of Respiratory and Critical Care Medicine Respiratory Infection and Intervention Laboratory of Frontiers Science Center for Disease\u2010Related Molecular Network State Key Laboratory of Biotherapy West China Hospital of Sichuan University  Chengdu 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Respiratory Infection and Intervention Laboratory of Frontiers Science Center for Disease\u2010Related Molecular Network State Key Laboratory of Biotherapy West China Hospital of Sichuan University  Chengdu China"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2022,1,10]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro.2017.126"},{"key":"e_1_2_11_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tim.2021.01.008"},{"key":"e_1_2_11_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41586-018-0498-z"},{"key":"e_1_2_11_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.biotechadv.2019.107468"},{"key":"e_1_2_11_6_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41579\u2010021\u201000597\u20106"},{"key":"e_1_2_11_7_1","article-title":"Microbial extracellular electron transfer and strategies for engineering electroactive microorganisms","author":"Zhao 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