7fh4

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7fh4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paramecium_bursaria_Chlorella_virus_1 Paramecium bursaria Chlorella virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FH4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7fh4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paramecium_bursaria_Chlorella_virus_1 Paramecium bursaria Chlorella virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FH4 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCM:2-DEOXYCYTIDINE-5-MONOPHOSPHATE'>DCM</scene>, <scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.996&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCM:2-DEOXYCYTIDINE-5-MONOPHOSPHATE'>DCM</scene>, <scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7fh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fh4 OCA], [https://pdbe.org/7fh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fh4 RCSB], [https://www.ebi.ac.uk/pdbsum/7fh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fh4 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7fh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fh4 OCA], [https://pdbe.org/7fh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fh4 RCSB], [https://www.ebi.ac.uk/pdbsum/7fh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fh4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/O41078_PBCV1 O41078_PBCV1]]
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[https://www.uniprot.org/uniprot/O41078_PBCV1 O41078_PBCV1]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:35764100</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7fh4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

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

PDB ID 7fh4

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