5wm1: Difference between revisions

Revision as of 10:18, 25 October 2017

Structure of the 10S (+)-trans-BP-dG modified Rev1 ternary complexStructure of the 10S (+)-trans-BP-dG modified Rev1 ternary complex

Structural highlights

5wm1 is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[REV1_YEAST] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis.^[1] ^[2] ^[3]

References

↑ Nelson JR, Lawrence CW, Hinkle DC. Deoxycytidyl transferase activity of yeast REV1 protein. Nature. 1996 Aug 22;382(6593):729-31. PMID:8751446 doi:10.1038/382729a0
↑ Haracska L, Unk I, Johnson RE, Johansson E, Burgers PM, Prakash S, Prakash L. Roles of yeast DNA polymerases delta and zeta and of Rev1 in the bypass of abasic sites. Genes Dev. 2001 Apr 15;15(8):945-54. PMID:11316789 doi:10.1101/gad.882301
↑ Zhang H, Chatterjee A, Singh KK. Saccharomyces cerevisiae polymerase zeta functions in mitochondria. Genetics. 2006 Apr;172(4):2683-8. Epub 2006 Feb 1. PMID:16452144 doi:genetics.105.051029

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OCA

[1] Nelson JR, Lawrence CW, Hinkle DC. Deoxycytidyl transferase activity of yeast REV1 protein. Nature. 1996 Aug 22;382(6593):729-31. PMID:8751446 doi:10.1038/382729a0

[2] Haracska L, Unk I, Johnson RE, Johansson E, Burgers PM, Prakash S, Prakash L. Roles of yeast DNA polymerases delta and zeta and of Rev1 in the bypass of abasic sites. Genes Dev. 2001 Apr 15;15(8):945-54. PMID:11316789 doi:10.1101/gad.882301

[3] Zhang H, Chatterjee A, Singh KK. Saccharomyces cerevisiae polymerase zeta functions in mitochondria. Genetics. 2006 Apr;172(4):2683-8. Epub 2006 Feb 1. PMID:16452144 doi:genetics.105.051029

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5wm1 is ON HOLD  until Paper Publication
+==Structure of the 10S (+)-trans-BP-dG modified Rev1 ternary complex==
+<StructureSection load='5wm1' size='340' side='right' caption='[[5wm1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5wm1]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WM1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WM1 FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BAP:1,2,3-TRIHYDROXY-1,2,3,4-TETRAHYDROBENZO[A]PYRENE'>BAP</scene>, <scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DDG:2,3-DIDEOXY-GUANOSINE-5-MONOPHOSPHATE'>DDG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wm1 OCA], [http://pdbe.org/5wm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wm1 RCSB], [http://www.ebi.ac.uk/pdbsum/5wm1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wm1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/REV1_YEAST REV1_YEAST]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis.<ref>PMID:8751446</ref> <ref>PMID:11316789</ref> <ref>PMID:16452144</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Aggarwal, A K]]
+[[Category: Geacintov, N E]]
+[[Category: Kolbanovsky, A]]
+[[Category: Landes, H]]
+[[Category: Rechkoblit, O]]
+[[Category: Dna binding protein]]
+[[Category: Transferase-dna complex]]

5wm1: Difference between revisions

Revision as of 10:18, 25 October 2017

Structure of the 10S (+)-trans-BP-dG modified Rev1 ternary complexStructure of the 10S (+)-trans-BP-dG modified Rev1 ternary complex

Structural highlights

Function

References

Contents

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5wm1: Difference between revisions

Revision as of 10:18, 25 October 2017

Structure of the 10S (+)-trans-BP-dG modified Rev1 ternary complexStructure of the 10S (+)-trans-BP-dG modified Rev1 ternary complex

Structural highlights

Function

References

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