2cg9 | pdb_00002cg9

CRYSTAL STRUCTURE OF AN HSP90-SBA1 CLOSED CHAPERONE COMPLEX

spinqualitylabelsall models 2cg9, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cg9 is a 4 chain structure with sequence from Saccharomyces cerevisiae. The December 2008 RCSB PDB Molecule of the Month feature on Hsp90 by David Goodsell is 10.2210/rcsb_pdb/mom_2008_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP Related: 1a4h, 1ah6, 1ah8, 1am1, 1amw, 1bgq, 1hk7, 1us7, 1usu, 1usv, 2akp, 2brc, 2bre, 2cge Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Hsp90 (heat shock protein of 90 kDa) is a ubiquitous molecular chaperone responsible for the assembly and regulation of many eukaryotic signalling systems and is an emerging target for rational chemotherapy of many cancers. Although the structures of isolated domains of Hsp90 have been determined, the arrangement and ATP-dependent dynamics of these in the full Hsp90 dimer have been elusive and contentious. Here we present the crystal structure of full-length yeast Hsp90 in complex with an ATP analogue and the co-chaperone p23/Sba1. The structure reveals the complex architecture of the 'closed' state of the Hsp90 chaperone, the extensive interactions between domains and between protein chains, the detailed conformational changes in the amino-terminal domain that accompany ATP binding, and the structural basis for stabilization of the closed state by p23/Sba1. Contrary to expectations, the closed Hsp90 would not enclose its client proteins but provides a bipartite binding surface whose formation and disruption are coupled to the chaperone ATPase cycle. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex.,Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH Nature. 2006 Apr 20;440(7087):1013-7. PMID:16625188 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Proteins

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