2BGZ

ATOMIC MODEL OF THE BACTERIAL FLAGELLAR BASED ON DOCKING AN X-RAY DERIVED HOOK STRUCTURE INTO AN EM MAP.

2BGZ の概要

• エントリーDOI: 10.2210/pdb2bgz/pdb
• 関連するPDBエントリー: 1WLG 2BGY
• EMDBエントリー: 1132
• 分子名称: FLAGELLAR HOOK PROTEIN FLGE (1 entity in total)
• 機能のキーワード: motor protein, bacterial motiility, bacterial flagellar hook, flagellum
• 由来する生物種: SALMONELLA TYPHIMURIUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31335.08

構造登録者

Shaikh, T.R.,Thomas, D.R.,Chen, J.Z.,Samatey, F.A.,Matsunami, H.,Imada, K.,Namba, K.,Derosier, D.J. (登録日: 2005-01-06, 公開日: 2005-01-27, 最終更新日: 2024-05-08)

主引用文献

Shaikh, T.R.,Thomas, D.R.,Chen, J.Z.,Samatey, F.A.,Matsunami, H.,Imada, K.,Namba, K.,Derosier, D.J.
A Partial Atomic Structure for the Flagellar Hook of Salmonella Typhimurium.
Proc.Natl.Acad.Sci.USA, 102:1023-, 2005

PubMed Abstract: The axial proteins of the bacterial flagellum function as a drive shaft, universal joint, and propeller driven by the flagellar rotary motor; they also form the putative protein export channel. The N- and C-terminal sequences of the eight axial proteins were predicted to form interlocking alpha-domains generating an axial tube. We report on an approximately 1-nm resolution map of the hook from Salmonella typhimurium, which reveals such a tube made from interdigitated, 1-nm rod-like densities similar to those seen in maps of the filament. Atomic models for the two outer domains of the hook subunit were docked into the corresponding outermost features of the map. The N and C termini of the hook subunit fragment are positioned next to each other and face toward the axis of the hook. The placement of these termini would permit the residues missing in the fragment to form the rod-like features that form the core domain of the hook. We also fit the hook atomic model to an approximately 2-nm resolution map of the hook from Caulobacter crescentus. The hook protein sequence from C. crescentus is largely homologous to that of S. typhimurium except for a large insertion (20 kDa). According to difference maps and our fitting, this insertion is found on the outer surface of the hook, consistent with our modeling of the hook.

PubMed: 15657146
DOI: 10.1073/PNAS.0409020102

実験手法

ELECTRON MICROSCOPY (9 Å)