1ORY

FLAGELLAR EXPORT CHAPERONE IN COMPLEX WITH ITS COGNATE BINDING PARTNER

1ORY の概要

• エントリーDOI: 10.2210/pdb1ory/pdb
• 関連するPDBエントリー: 1ORY
• 分子名称: flagellar protein FliS, Flagellin, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: flagellar chaperone, cytosolic export chaperone, flagellin, flis, flic, chaperone
• 由来する生物種: Aquifex aeolicus; 詳細
• 細胞内の位置: Secreted: O67803
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21897.89

構造登録者

Evdokimov, A.G.,Phan, J.,Tropea, J.E.,Routzahn, K.M.,Peters III, H.K.,Pokross, M.,Waugh, D.S. (登録日: 2003-03-17, 公開日: 2003-09-16, 最終更新日: 2023-11-29)

主引用文献

Evdokimov, A.G.,Phan, J.,Tropea, J.E.,Routzahn, K.M.,Peters III, H.K.,Pokross, M.,Waugh, D.S.
Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion
Nat.Struct.Biol., 10:789-793, 2003

PubMed Abstract: Assembly of the bacterial flagellum and type III secretion in pathogenic bacteria require cytosolic export chaperones that interact with mobile components to facilitate their secretion. Although their amino acid sequences are not conserved, the structures of several type III secretion chaperones revealed striking similarities between their folds and modes of substrate recognition. Here, we report the first crystallographic structure of a flagellar export chaperone, Aquifex aeolicus FliS. FliS adopts a novel fold that is clearly distinct from those of the type III secretion chaperones, indicating that they do not share a common evolutionary origin. However, the structure of FliS in complex with a fragment of FliC (flagellin) reveals that, like the type III secretion chaperones, flagellar export chaperones bind their target proteins in extended conformation and suggests that this mode of recognition may be widely used in bacteria.

PubMed: 12958592
DOI: 10.1038/nsb982

実験手法

X-RAY DIFFRACTION (2.45 Å)