4be8 | pdb_00004be8

NEDD4 HECT A889F structure

spinqualitylabelsall models 4be8, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4be8 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4bbn Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Homologous to E6-AP C terminus (HECT) E3 ligases recognize and directly catalyze ligation of ubiquitin (Ub) to their substrates. Molecular details of this process remain unknown. We report the first structure, to our knowledge, of a Ub-loaded E3, the human neural precursor cell-expressed developmentally downregulated protein 4 (Nedd4). The HECTNedd4~Ub transitory intermediate provides a structural basis for the proposed sequential addition mechanism. The donor Ub, transferred from the E2, is bound to the Nedd4 C lobe with its C-terminal tail locked in an extended conformation, primed for catalysis. We provide evidence that the Nedd4-family members are Lys63-specific enzymes whose catalysis is mediated by an essential C-terminal acidic residue. Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming.,Maspero E, Valentini E, Mari S, Cecatiello V, Soffientini P, Pasqualato S, Polo S Nat Struct Mol Biol. 2013 May 5. doi: 10.1038/nsmb.2566. PMID:23644597 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ubiquitin protein ligase

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