3OLM

Structure and Function of a Ubiquitin Binding Site within the Catalytic Domain of a HECT Ubiquitin Ligase

Summary for 3OLM

• Entry DOI: 10.2210/pdb3olm/pdb
• Descriptor: E3 ubiquitin-protein ligase RSP5, Ubiquitin (3 entities in total)
• Functional Keywords: ubiquitin e3 ligase, ligase
• Biological source: Saccharomyces cerevisiae (yeast); More
• Cellular location: Cytoplasm: P39940; Cytoplasm (By similarity): P0CG63
• Total number of polymer chains: 2
• Total formula weight: 59207.69

Authors

Kim, H.C.,Steffen, A.,Chen, J.,Huibregtse, J.M. (deposition date: 2010-08-26, release date: 2011-03-23, Last modification date: 2023-09-06)

Primary citation

Kim, H.C.,Steffen, A.M.,Oldham, M.L.,Chen, J.,Huibregtse, J.M.
Structure and function of a HECT domain ubiquitin-binding site.
Embo Rep., 12:334-341, 2011

PubMed Abstract: The Rsp5 ubiquitin ligase contains a non-covalent binding site for ubiquitin within the amino-terminal lobe (N-lobe) of the HECT domain, and the X-ray crystal structure of the HECT-ubiquitin complex has been determined. Hydrophobic patch residues of ubiquitin (L8, I44, V70) were crucial for interaction with Rsp5, and amino-acid alterations at the Rsp5-binding interface resulted in defects in polyubiquitination. Our results support a model in which the N-lobe-binding site acts to localize and orient the distal end of the ubiquitin chain to promote conjugation of the next ubiquitin molecule.

PubMed: 21399621
DOI: 10.1038/embor.2011.23

Experimental method

X-RAY DIFFRACTION (2.495 Å)