2jki | pdb_00002jki
COMPLEX OF HSP90 N-TERMINAL AND SGT1 CS DOMAIN
Structural highlights
Function[Q84LL4_ARATH] Functions in R gene-mediated resistance, but participates in a lower extent than SGT1B to RPP5-mediated resistance. Not required for RPM1, RPS2, RPS4 and RPS5-mediated resistance. Probably required for SCF-mediated ubiquitination, by coupling HSP90 to SCF complex for ubiquitination of HSP90 client proteins.[1] 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 PubMedSgt1 is an adaptor protein implicated in a variety of processes, including formation of the kinetochore complex in yeast, and regulation of innate immunity systems in plants and animals. Sgt1 has been found to associate with SCF E3 ubiquitin ligases, the CBF3 kinetochore complex, plant R proteins and related animal Nod-like receptors, and with the Hsp90 molecular chaperone. We have determined the crystal structure of the core Hsp90-Sgt1 complex, revealing a distinct site of interaction on the Hsp90 N-terminal domain. Using the structure, we developed mutations in Sgt1 interfacial residues, which specifically abrogate interaction with Hsp90, and disrupt Sgt1-dependent functions in vivo, in plants and yeast. We show that Sgt1 bridges the Hsp90 molecular chaperone system to the substrate-specific arm of SCF ubiquitin ligase complexes, suggesting a role in SCF assembly and regulation, and providing multiple complementary routes for ubiquitination of Hsp90 client proteins. Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes.,Zhang M, Boter M, Li K, Kadota Y, Panaretou B, Prodromou C, Shirasu K, Pearl LH EMBO J. 2008 Oct 22;27(20):2789-98. Epub 2008 Sep 25. PMID:18818696[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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