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-Structure paper
タイトル | Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 3396, Year 2020 |
掲載日 | 2020年7月7日 |
著者 | Yong Zi Tan / José Rodrigues / James E Keener / Ruixiang Blake Zheng / Richard Brunton / Brian Kloss / Sabrina I Giacometti / Ana L Rosário / Lei Zhang / Michael Niederweis / Oliver B Clarke / Todd L Lowary / Michael T Marty / Margarida Archer / Clinton S Potter / Bridget Carragher / Filippo Mancia / |
PubMed 要旨 | Arabinosyltransferase B (EmbB) belongs to a family of membrane-bound glycosyltransferases that build the lipidated polysaccharides of the mycobacterial cell envelope, and are targets of anti- ...Arabinosyltransferase B (EmbB) belongs to a family of membrane-bound glycosyltransferases that build the lipidated polysaccharides of the mycobacterial cell envelope, and are targets of anti-tuberculosis drug ethambutol. We present the 3.3 Å resolution single-particle cryo-electron microscopy structure of Mycobacterium smegmatis EmbB, providing insights on substrate binding and reaction mechanism. Mutations that confer ethambutol resistance map mostly around the putative active site, suggesting this to be the location of drug binding. |
リンク | Nat Commun / PubMed:32636380 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.3 Å |
構造データ | EMDB-21983, PDB-6x0o: |
化合物 | ChemComp-CA: ChemComp-LHG: |
由来 |
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キーワード | MEMBRANE PROTEIN / Glycosyltransferase / nanodisc |