7fh4

Chlorovirus PBCV-1 bi-functional dCMP/dCTP deaminase bi-DCD

spinqualitylabelsall models 7fh4, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7fh4 is a 2 chain structure with sequence from Paramecium bursaria Chlorella virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.996Å Ligands: DCM, DCP, MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O41078_PBCV1 Publication Abstract from PubMed 2-Deoxycytidylate deaminase (dCD) is a member of the zinc-dependent cytidine deaminase family features in its allosterically regulated mechanism by dCTP and dTTP. The large double-stranded DNA-containing chlorovirus PBCV-1 encodes a dCD family enzyme PBCV1dCD that was reported to be able to deaminize both dCMP and dCTP, which makes PBCV1dCD unique in the dCD family proteins. In this study, we report the crystal structure of PBCV1dCD in complex with dCTP/dCMP and dTTP/dTMP, respectively. We further proved the ability of PBCV1dCD in the deamination of dCDP, which makes PBCV1dCD a multi-functional deaminase. The structural basis for the versatility of PBCV1dCD is analyzed and discussed, with the finding of a unique Trp121 residue key to the deamination and substrate binding ability. Our findings may broaden the understanding of dCD family proteins and provide novel insights into the multi-functional enzyme. Structural basis of a multi-functional deaminase in chlorovirus PBCV-1.,Li YH, Hou HF, Geng Z, Zhang H, She Z, Dong YH Arch Biochem Biophys. 2022 Sep 30;727:109339. doi: 10.1016/j.abb.2022.109339. , Epub 2022 Jun 25. PMID:35764100 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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