2XCM
COMPLEX OF HSP90 N-TERMINAL, SGT1 CS AND RAR1 CHORD2 DOMAIN
Summary for 2XCM
| Entry DOI | 10.2210/pdb2xcm/pdb |
| Related | 2JKI |
| Descriptor | CYTOSOLIC HEAT SHOCK PROTEIN 90, SGT1-LIKE PROTEIN, RAR1, ... (7 entities in total) |
| Functional Keywords | chaperone-protein binding complex, stress response, chaperone/protein binding |
| Biological source | HORDEUM VULGARE More |
| Total number of polymer chains | 6 |
| Total formula weight | 86947.86 |
| Authors | Zhang, M.,Pearl, L.H. (deposition date: 2010-04-23, release date: 2010-08-11, Last modification date: 2023-12-20) |
| Primary citation | 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 Cited by 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: 20670895DOI: 10.1016/J.MOLCEL.2010.05.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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