Structural highlights
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 Jun 25;727:109339. doi: 10.1016/j.abb.2022.109339. PMID:35764100[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li YH, Hou HF, Geng Z, Zhang H, She Z, Dong YH. Structural basis of a multi-functional deaminase in chlorovirus PBCV-1. Arch Biochem Biophys. 2022 Jun 25;727:109339. doi: 10.1016/j.abb.2022.109339. PMID:35764100 doi:http://dx.doi.org/10.1016/j.abb.2022.109339
