7FH4

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

Summary for 7FH4

• Entry DOI: 10.2210/pdb7fh4/pdb
• Descriptor: CMP/dCMP-type deaminase domain-containing protein, 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE, 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: deaminase, bi-function, dcmp, dctp, biosynthetic protein
• Biological source: Paramecium bursaria Chlorella virus 1 (PBCV-1)
• Total number of polymer chains: 2
• Total formula weight: 33546.31

Authors

She, Z. (deposition date: 2021-07-29, release date: 2022-07-06, Last modification date: 2024-05-29)

Primary citation

Li, Y.H.,Hou, H.F.,Geng, Z.,Zhang, H.,She, Z.,Dong, Y.H.
Structural basis of a multi-functional deaminase in chlorovirus PBCV-1.
Arch.Biochem.Biophys., 727:109339-109339, 2022

PubMed Abstract: 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.

PubMed: 35764100
DOI: 10.1016/j.abb.2022.109339

Experimental method

X-RAY DIFFRACTION (1.996 Å)