3X3N
Crystal structure of EccB1 of Mycobacterium tuberculosis in spacegroup P21
3X3N の概要
エントリーDOI | 10.2210/pdb3x3n/pdb |
関連するPDBエントリー | 3X3M |
分子名称 | ESX-1 secretion system protein EccB1, CALCIUM ION (3 entities in total) |
機能のキーワード | alpha-beta-alpha sandwich, beta-sheet, atpase, protein transport |
由来する生物種 | Mycobacterium tuberculosis |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 46300.74 |
構造登録者 | Zhang, X.L.,Li, D.F.,Zhang, X.E.,Bi, L.J.,Wang, D.C. (登録日: 2015-01-24, 公開日: 2015-12-09, 最終更新日: 2022-08-24) |
主引用文献 | Zhang, X.L.,Li, D.F.,Fleming, J.,Wang, L.W.,Zhou, Y.,Wang, D.C.,Zhang, X.E.,Bi, L.J. Core component EccB1 of the Mycobacterium tuberculosis type VII secretion system is a periplasmic ATPase. Faseb J., 29:4804-4814, 2015 Cited by PubMed Abstract: Pathogenic mycobacteria transport virulence factors across their complex cell wall via a type VII secretion system (T7SS)/early secreted antigenic target-6 of kDa secretion system (ESX). ESX conserved component (Ecc) B, a core component of the T7SS architecture, is predicted to be a membrane bound protein, but little is known about its structure and function. Here, we characterize EccB1, showing that it is an ATPase with no sequence or structural homology to other ATPases located in the cell envelope of Mycobacterium tuberculosis H37Rv. We obtained the crystal structure of an EccB1-ΔN72 truncated transmembrane helix and performed modeling and ATP docking studies, showing that EccB1 likely exists as a hexamer. Sequence alignment and ATPase activity determination of EccB1 homologues indicated the presence of 3 conserved motifs in the N- and C-terminals of EccB1-ΔN72 that assemble together between 2 membrane proximal domains of the EccB1-ΔN72 monomer. Models of the EccB1 hexamer show that 2 of the conserved motifs are involved in ATPase activity and form an ATP binding pocket located on the surface of 2 adjacent molecules. Our results suggest that EccB may act as the energy provider in the transport of T7SS virulence factors and may be involved in the formation of a channel across the mycomembrane. PubMed: 26396239DOI: 10.1096/fj.15-270843 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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