3olm | pdb_00003olm

Structure and Function of a Ubiquitin Binding Site within the Catalytic Domain of a HECT Ubiquitin Ligase

spinqualitylabelsall models 3olm, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3olm is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: RSP5, MDP1, NPI1, YER125W, SYGP-ORF41 (Saccharomyces cerevisiae), UBI4, SCD2, YLL039C (Saccharomyces cerevisiae) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The Rsp5 ubiquitin ligase contains a non-covalent binding site for ubiquitin within the amino-terminal lobe (N-lobe) of the HECT domain, and the X-ray crystal structure of the HECT-ubiquitin complex has been determined. Hydrophobic patch residues of ubiquitin (L8, I44, V70) were crucial for interaction with Rsp5, and amino-acid alterations at the Rsp5-binding interface resulted in defects in polyubiquitination. Our results support a model in which the N-lobe-binding site acts to localize and orient the distal end of the ubiquitin chain to promote conjugation of the next ubiquitin molecule. Structure and function of a HECT domain ubiquitin-binding site.,Kim HC, Steffen AM, Oldham ML, Chen J, Huibregtse JM EMBO Rep. 2011 Mar 11. PMID:21399621 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ubiquitin protein ligase

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