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Structure and function of a HECT domain ubiquitin-binding site.

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.

SUBMITTER: Kim HC

PROVIDER: S-EPMC3077248 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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Structure and function of a HECT domain ubiquitin-binding site.

Kim Hyung Cheol HC Steffen Alanna M AM Oldham Michael L ML Chen Jue J Huibregtse Jon M JM

EMBO reports 20110311 4

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 ori ...[more]

PMID: 21399621

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