2xbb | pdb_00002xbb

NEDD4 HECT:UB COMPLEX

spinqualitylabelsall models 2xbb, resolution 2.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xbb is a 4 chain structure with sequence from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Related: 2xbf Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation.,Maspero E, Mari S, Valentini E, Musacchio A, Fish A, Pasqualato S, Polo S EMBO Rep. 2011 Mar 11. PMID:21399620 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ubiquitin protein ligase

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