2c2l
CRYSTAL STRUCTURE OF THE CHIP U-BOX E3 UBIQUITIN LIGASE
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OverviewOverview
CHIP is a dimeric U box E3 ubiquitin ligase that binds Hsp90 and/or Hsp70, via its TPR-domain, facilitating ubiquitylation of chaperone bound client, proteins. We have determined the crystal structure of CHIP bound to an, Hsp90 C-terminal decapeptide. The structure explains how CHIP associates, with either chaperone type and reveals an unusual asymmetric homodimer in, which the protomers adopt radically different conformations. Additionally, we identified CHIP as a functional partner of Ubc13-Uev1a in formation of, Lys63-linked polyubiquitin chains, extending CHIP's roles into ubiquitin, regulation as well as targeted destruction. The structure of Ubc13-Uev1a, bound to the CHIP U box domain defines the basis for selective cooperation, of CHIP with specific ubiquitin-conjugating enzymes. Remarkably, the, asymmetric arrangement of the TPR domains in the CHIP dimer occludes one, Ubc binding site, so that CHIP operates with half-of-sites activity, providing an elegant means for coupling a dimeric chaperone to a single, ubiquitylation system.
About this StructureAbout this Structure
2C2L is a Protein complex structure of sequences from Mus musculus with SO4 and NI as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex., Zhang M, Windheim M, Roe SM, Peggie M, Cohen P, Prodromou C, Pearl LH, Mol Cell. 2005 Nov 23;20(4):525-38. PMID:16307917
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