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 Repjournal_title
EMBO reportsauthors
Maspero E,Mari S,Valentini E,Musacchio A,Fish A,Pasqualato S,Polo Sdoi
10.1038/embor.2011.21subject
Has Abstractpub_date
2011-04-01 00:00:00pages
342-9issue
4eissn
1469-221Xissn
1469-3178pii
embor201121journal_volume
12pub_type
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