6nyd

Crystal Structure of S. cerevisiae Ubc3 (Cdc34)

spinqualitylabelsall models 6nyd, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nyd is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: ACT, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UBC3_YEAST Catalyzes the covalent attachment of ubiquitin to other proteins. Capable, in vitro, to ubiquitinate histone H2A. Mediates the initiation of DNA replication (transition of G1 to S phase in cell cycle). Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the regulation of methionine biosynthesis genes and in the degradation of CDC6 together with CDC4 and CDC53. Publication Abstract from PubMed Ubiquitin (Ub) signaling requires the sequential interactions and activities of three enzymes, E1, E2, and E3. Cdc34 is an E2 that plays a key role in regulating cell cycle progression and requires unique structural elements to function. The molecular basis by which Cdc34 engages its E1 and the structural mechanisms by which its unique C-terminal extension functions in Cdc34 activity are unknown. Here, we present crystal structures of Cdc34 alone and in complex with E1, and a Cdc34~Ub thioester mimetic that represents the product of Uba1-Cdc34 Ub transthiolation. These structures reveal conformational changes in Uba1 and Cdc34 and a unique binding mode that are required for transthiolation. The Cdc34~Ub structure reveals contacts between the Cdc34 C-terminal extension and Ub that stabilize Cdc34~Ub in a closed conformation and are critical for Ub discharge. Altogether, our structural, biochemical, and cell-based studies provide insights into the molecular mechanisms by which Cdc34 function in cells. Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34.,Williams KM, Qie S, Atkison JH, Salazar-Arango S, Alan Diehl J, Olsen SK Nat Commun. 2019 Jul 24;10(1):3296. doi: 10.1038/s41467-019-11061-8. PMID:31341161 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 3D structures of ubiquitin conjugating enzyme

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