2XCM

COMPLEX OF HSP90 N-TERMINAL, SGT1 CS AND RAR1 CHORD2 DOMAIN

2XCM の概要

• エントリーDOI: 10.2210/pdb2xcm/pdb
• 関連するPDBエントリー: 2JKI
• 分子名称: CYTOSOLIC HEAT SHOCK PROTEIN 90, SGT1-LIKE PROTEIN, RAR1, ... (7 entities in total)
• 機能のキーワード: chaperone-protein binding complex, stress response, chaperone/protein binding
• 由来する生物種: HORDEUM VULGARE; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 86947.86

構造登録者

Zhang, M.,Pearl, L.H. (登録日: 2010-04-23, 公開日: 2010-08-11, 最終更新日: 2023-12-20)

主引用文献

Zhang, M.,Kadota, Y.,Prodromou, C.,Shirasu, K.,Pearl, L.H.
Structural Basis for Assembly of Hsp90-Sgt1-Chord Protein Complexes: Implications for Chaperoning of Nlr Innate Immunity Receptors
Mol.Cell, 39:269-, 2010

PubMed Abstract: Hsp90-mediated function of NLR receptors in plant and animal innate immunity depends on the cochaperone Sgt1 and, at least in plants, on a cysteine- and histidine-rich domains (CHORD)-containing protein Rar1. Functionally, CHORD domains are associated with CS domains, either within the same protein, as in the mammalian melusin and Chp1, or in separate but interacting proteins, as in the plant Rar1 and Sgt1. Both CHORD and CS domains are independently capable of interacting with the molecular chaperone Hsp90 and can coexist in complexes with Hsp90. We have now determined the structure of an Hsp90-CS-CHORD ternary complex, providing a framework for understanding the dynamic nature of Hsp90-Rar1-Sgt1 complexes. Mutational and biochemical analyses define the architecture of the ternary complex that recruits nucleotide-binding leucine-rich repeat receptors (NLRs) by manipulating the structural elements to control the ATPase-dependent conformational cycle of the chaperone.

PubMed: 20670895
DOI: 10.1016/J.MOLCEL.2010.05.010

実験手法

X-RAY DIFFRACTION (2.2 Å)