2BHO

Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycT

2BHO の概要

• エントリーDOI: 10.2210/pdb2bho/pdb
• 関連するPDBエントリー: 2BSH 2BSI 2BSJ
• 分子名称: CHAPERONE PROTEIN SYCT, PLATINUM (II) ION (3 entities in total)
• 機能のキーワード: yersinia, chaperone, secretion
• 由来する生物種: YERSINIA ENTEROCOLITICA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15375.08

構造登録者

Groll, M.,Wilharm, G. (登録日: 2005-01-15, 公開日: 2005-07-06, 最終更新日: 2024-05-08)

主引用文献

Locher, M.,Lehnert, B.,Krauss, K.,Heesemann, J.,Groll, M.,Wilharm, G.
Crystal Structure of the Yersinia Enterocolitica Type III Secretion Chaperone Syct
J.Biol.Chem., 280:31149-, 2005

PubMed Abstract: Several Gram-negative pathogens deploy type III secretion systems (TTSSs) as molecular syringes to inject effector proteins into host cells. Prior to secretion, some of these effectors are accompanied by specific type III secretion chaperones. The Yersinia enterocolitica TTSS chaperone SycT escorts the effector YopT, a cysteine protease that inactivates the small GTPase RhoA of targeted host cells. We solved the crystal structure of SycT at 2.5 angstroms resolution. Despite limited sequence similarity among TTSS chaperones, the SycT structure revealed a global fold similar to that exhibited by other structurally solved TTSS chaperones. The dimerization domain of SycT, however, differed from that of all other known TTSS chaperone structures. Thus, the dimerization domain of TTSS chaperones does not likely serve as a general recognition pattern for downstream processing of effector/chaperone complexes. Yersinia Yop effectors are bound to their specific Syc chaperones close to the Yop N termini, distinct from their catalytic domains. Here, we showed that the catalytically inactive YopT(C139S) is reduced in its ability to bind SycT, suggesting an ancillary interaction between YopT and SycT. This interaction could maintain the protease inactive prior to secretion or could influence the secretion competence and folding of YopT.

PubMed: 16000312
DOI: 10.1074/JBC.M500603200

実験手法

X-RAY DIFFRACTION (2.6 Å)