2fuh | pdb_00002fuh

Solution Structure of the UbcH5c/Ub Non-covalent Complex

spinqualitylabelsall models 2fuh, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2fuh is a 2 chain structure with sequence from Homo sapiens and Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: UBE2D3, UBCH5C (Homo sapiens), Rps27a, Uba80, Ubcep1 (Rattus norvegicus) Activity: Ubiquitin--protein ligase, with EC number 6.3.2.19 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Protein ubiquitination is a powerful regulatory modification that influences nearly every aspect of eukaryotic cell biology. The general pathway for ubiquitin (Ub) modification requires the sequential activities of a Ub-activating enzyme (E1), a Ub transfer enzyme (E2), and a Ub ligase (E3). The E2 must recognize both the E1 and a cognate E3 in addition to carrying activated Ub. These central functions are performed by a topologically conserved alpha/beta-fold core domain of approximately 150 residues shared by all E2s. However, as presented herein, the UbcH5 family of E2s can also bind Ub noncovalently on a surface well removed from the E2 active site. We present the solution structure of the UbcH5c/Ub noncovalent complex and demonstrate that this noncovalent interaction permits self-assembly of activated UbcH5c approximately Ub molecules. Self-assembly has profound consequences for the processive formation of polyubiquitin (poly-Ub) chains in ubiquitination reactions directed by the breast and ovarian cancer tumor susceptibility protein BRCA1. A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination.,Brzovic PS, Lissounov A, Christensen DE, Hoyt DW, Klevit RE Mol Cell. 2006 Mar 17;21(6):873-80. PMID:16543155 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ubiquitin Ubiquitin conjugating enzyme

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