Structure and function of a HECT domain ubiquitin-binding site.
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.
Mesh Terms:
Crystallography, X-Ray, Endosomal Sorting Complexes Required for Transport, Protein Binding, Protein Structure, Tertiary, Saccharomyces cerevisiae Proteins, Ubiquitin, Ubiquitin-Protein Ligase Complexes, Ubiquitination
Crystallography, X-Ray, Endosomal Sorting Complexes Required for Transport, Protein Binding, Protein Structure, Tertiary, Saccharomyces cerevisiae Proteins, Ubiquitin, Ubiquitin-Protein Ligase Complexes, Ubiquitination
EMBO Rep.
Date: Apr. 01, 2011
PubMed ID: 21399621
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