7E1V
Cryo-EM structure of apo hybrid respiratory supercomplex consisting of Mycobacterium tuberculosis complexIII and Mycobacterium smegmatis complexIV
7E1V の概要
エントリーDOI | 10.2210/pdb7e1v/pdb |
EMDBエントリー | 30943 |
分子名称 | Cytochrome c oxidase subunit 2, Cytochrome bc1 complex cytochrome c subunit, COPPER (II) ION, ... (20 entities in total) |
機能のキーワード | mycobacterium smegmatis, mycobacterium tuberculosis, complexiii, complexiv, electron transport, anti-tb drugs, oxidoreductase |
由来する生物種 | Mycobacterium tuberculosis H37Rv 詳細 |
タンパク質・核酸の鎖数 | 20 |
化学式量合計 | 672680.63 |
構造登録者 | |
主引用文献 | Zhou, S.,Wang, W.,Zhou, X.,Zhang, Y.,Lai, Y.,Tang, Y.,Xu, J.,Li, D.,Lin, J.,Yang, X.,Ran, T.,Chen, H.,Guddat, L.W.,Wang, Q.,Gao, Y.,Rao, Z.,Gong, H. Structure of Mycobacterium tuberculosis cytochrome bcc in complex with Q203 and TB47, two anti-TB drug candidates. Elife, 10:-, 2021 Cited by PubMed Abstract: Pathogenic mycobacteria pose a sustained threat to global human health. Recently, cytochrome complexes have gained interest as targets for antibiotic drug development. However, there is currently no structural information for the cytochrome complex from these pathogenic mycobacteria. Here, we report the structures of cytochrome alone (2.68 Å resolution) and in complex with clinical drug candidates Q203 (2.67 Å resolution) and TB47 (2.93 Å resolution) determined by single-particle cryo-electron microscopy. cytochrome forms a dimeric assembly with endogenous menaquinone/menaquinol bound at the quinone/quinol-binding pockets. We observe Q203 and TB47 bound at the quinol-binding site and stabilized by hydrogen bonds with the side chains of Thr and Glu, residues that are conserved across pathogenic mycobacteria. These high-resolution images provide a basis for the design of new mycobacterial cytochrome inhibitors that could be developed into broad-spectrum drugs to treat mycobacterial infections. PubMed: 34819223DOI: 10.7554/eLife.69418 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.68 Å) |
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