Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation.

Abstract:

:Several mechanisms have been proposed for the synthesis of substrate-linked ubiquitin chains. HECT ligases directly catalyse protein ubiquitination and have been found to non-covalently interact with ubiquitin. We report crystal structures of the Nedd4 HECT domain, alone and in complex with ubiquitin, which show a new binding mode involving two surfaces on ubiquitin and both subdomains of the HECT N-lobe. The structures suggest a model for HECT-to-substrate ubiquitin transfer, in which the growing chain on the substrate is kept close to the catalytic cysteine to promote processivity. Mutational analysis highlights differences between the processes of substrate polyubiquitination and self-ubiquitination.

journal_name

EMBO Rep

journal_title

EMBO reports

authors

Maspero E,Mari S,Valentini E,Musacchio A,Fish A,Pasqualato S,Polo S

doi

10.1038/embor.2011.21

subject

Has Abstract

pub_date

2011-04-01 00:00:00

pages

342-9

issue

4

eissn

1469-221X

issn

1469-3178

pii

embor201121

journal_volume

12

pub_type

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