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1zqt

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Revision as of 23:27, 10 September 2015

DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (0.01 MILLIMOLAR) AND ZNCL2 (0.02 MILLIMOLAR)

Structural highlights

1zqt is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	7ice, 7icf, 7icg, 7ich, 7ici, 7icj, 7ick, 7icl, 7icm, 7icn, 7ico, 7icp, 7icq, 7icr, 7ics, 7ict, 7icu, 7icv, 8ica, 8icb, 8icc, 8ice, 8icf, 8icg, 8ich, 8ici, 8icj, 8ick, 8icl, 8icm, 8icn, 8ico, 8icp, 8icq, 8icr, 8ics, 8ict, 8icu, 8icv, 8icw, 8icx, 8icy, 8icz, 9ica, 9icb, 9icc, 9ice, 9icf, 9icg, 9ich, 9ici, 9icj, 9ick, 9icl, 9icm, 9icn, 9ico, 9icp, 9icq, 9icr, 9ics, 9ict, 9icu, 9icv, 9icw, 9icx, 9icy, 1zqa, 1zqb, 1zqc, 1zqd, 1zqe, 1zqf, 1zqg, 1zqh, 1zqi, 1zqj, 1zqk, 1zql, 1zqm, 1zqn, 1zqo, 1zqp, 1zqq, 1zqr, 1zqs
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[DPOLB_HUMAN] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

When crystals of human DNA polymerase beta (pol beta) complexed with DNA [Pelletier, H., Sawaya, M. R., Wolfle, W., Wilson, S. H., & Kraut, J. (1996) Biochemistry 35, 12742-12761] are soaked in the presence of dATP and Mn2+, X-ray structural analysis shows that nucleotidyl transfer to the primer 3'-OH takes place directly in the crystals, even though the DNA is blunt-ended at the active site. Under similar crystal-soaking conditions, there is no evidence for a reaction when Mn2+ is replaced by Mg2+, which is thought to be the divalent metal ion utilized by most polymerases in vivo. These results suggest that one way Mn2+ may manifest its mutagenic effect on polymerases is by promoting greater reactivity than Mg2+ at the catalytic site, thereby allowing the nucleotidyl transfer reaction to take place with little or no regard to instructions from a template. Non-template-directed nucleotidyl transfer is also observed when pol beta-DNA cocrystals are soaked in the presence of dATP and Zn2+, but the reaction products differ in that the sugar moiety of the incorporated nucleotide appears distorted or otherwise cleaved, in agreement with reports that Zn2+ may act as a polymerase inhibitor rather than as a mutagen [Sirover, M. A., & Loeb, L. A. (1976) Science 194, 1434-1436]. Although no reaction is observed when crystals are soaked in the presence of dATP and other metal ions such as Ca2+, Co2+, Cr3+, or Ni2+, X-ray structural analyses show that these metal ions coordinate the triphosphate moiety of the nucleotide in a manner that differs from that observed with Mg2+. In addition, all metal ions tested, with the exception of Mg2+, promote a change in the side-chain position of aspartic acid 192, which is one of three highly conserved active-site carboxylate residues. Soaking experiments with nucleotides other than dATP (namely, dCTP, dGTP, dTTP, ATP, ddATP, ddCTP, AZT-TP, and dATP alpha S) reveal a non-base-specific binding site on pol beta for the triphosphate and sugar moieties of a nucleotide, suggesting a possible mechanism for nucleotide selectivity whereby triphosphate-sugar binding precedes a check for correct base pairing with the template.

A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase beta.,Pelletier H, Sawaya MR, Wolfle W, Wilson SH, Kraut J Biochemistry. 1996 Oct 1;35(39):12762-77. PMID:8841119^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bennett RA, Wilson DM 3rd, Wong D, Demple B. Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway. Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7166-9. PMID:9207062
↑ Matsumoto Y, Kim K, Katz DS, Feng JA. Catalytic center of DNA polymerase beta for excision of deoxyribose phosphate groups. Biochemistry. 1998 May 5;37(18):6456-64. PMID:9572863 doi:10.1021/bi9727545
↑ DeMott MS, Beyret E, Wong D, Bales BC, Hwang JT, Greenberg MM, Demple B. Covalent trapping of human DNA polymerase beta by the oxidative DNA lesion 2-deoxyribonolactone. J Biol Chem. 2002 Mar 8;277(10):7637-40. Epub 2002 Jan 22. PMID:11805079 doi:10.1074/jbc.C100577200
↑ Parsons JL, Dianova II, Khoronenkova SV, Edelmann MJ, Kessler BM, Dianov GL. USP47 is a deubiquitylating enzyme that regulates base excision repair by controlling steady-state levels of DNA polymerase beta. Mol Cell. 2011 Mar 4;41(5):609-15. doi: 10.1016/j.molcel.2011.02.016. PMID:21362556 doi:10.1016/j.molcel.2011.02.016
↑ Pelletier H, Sawaya MR, Wolfle W, Wilson SH, Kraut J. A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase beta. Biochemistry. 1996 Oct 1;35(39):12762-77. PMID:8841119 doi:http://dx.doi.org/10.1021/bi9529566

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zqt"

@@ Line 2: / Line 2: @@
 <StructureSection load='1zqt' size='340' side='right' caption='[[1zqt]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1zqt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZQT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1zqt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZQT FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[7ice|7ice]], [[7icf|7icf]], [[7icg|7icg]], [[7ich|7ich]], [[7ici|7ici]], [[7icj|7icj]], [[7ick|7ick]], [[7icl|7icl]], [[7icm|7icm]], [[7icn|7icn]], [[7ico|7ico]], [[7icp|7icp]], [[7icq|7icq]], [[7icr|7icr]], [[7ics|7ics]], [[7ict|7ict]], [[7icu|7icu]], [[7icv|7icv]], [[8ica|8ica]], [[8icb|8icb]], [[8icc|8icc]], [[8ice|8ice]], [[8icf|8icf]], [[8icg|8icg]], [[8ich|8ich]], [[8ici|8ici]], [[8icj|8icj]], [[8ick|8ick]], [[8icl|8icl]], [[8icm|8icm]], [[8icn|8icn]], [[8ico|8ico]], [[8icp|8icp]], [[8icq|8icq]], [[8icr|8icr]], [[8ics|8ics]], [[8ict|8ict]], [[8icu|8icu]], [[8icv|8icv]], [[8icw|8icw]], [[8icx|8icx]], [[8icy|8icy]], [[8icz|8icz]], [[9ica|9ica]], [[9icb|9icb]], [[9icc|9icc]], [[9ice|9ice]], [[9icf|9icf]], [[9icg|9icg]], [[9ich|9ich]], [[9ici|9ici]], [[9icj|9icj]], [[9ick|9ick]], [[9icl|9icl]], [[9icm|9icm]], [[9icn|9icn]], [[9ico|9ico]], [[9icp|9icp]], [[9icq|9icq]], [[9icr|9icr]], [[9ics|9ics]], [[9ict|9ict]], [[9icu|9icu]], [[9icv|9icv]], [[9icw|9icw]], [[9icx|9icx]], [[9icy|9icy]], [[1zqa|1zqa]], [[1zqb|1zqb]], [[1zqc|1zqc]], [[1zqd|1zqd]], [[1zqe|1zqe]], [[1zqf|1zqf]], [[1zqg|1zqg]], [[1zqh|1zqh]], [[1zqi|1zqi]], [[1zqj|1zqj]], [[1zqk|1zqk]], [[1zql|1zql]], [[1zqm|1zqm]], [[1zqn|1zqn]], [[1zqo|1zqo]], [[1zqp|1zqp]], [[1zqq|1zqq]], [[1zqr|1zqr]], [[1zqs|1zqs]]</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=1zqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zqt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zqt RCSB], [http://www.ebi.ac.uk/pdbsum/1zqt PDBsum]</span></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=1zqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zqt OCA], [http://pdbe.org/1zqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zqt RCSB], [http://www.ebi.ac.uk/pdbsum/1zqt PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN]] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1zqt" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 32: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Pelletier, H]]
 [[Category: Sawaya, M R]]

1zqt

From Proteopedia

Revision as of 23:27, 10 September 2015

DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7) COMPLEXED WITH SEVEN BASE PAIRS OF DNA; SOAKED IN THE PRESENCE OF DATP (0.01 MILLIMOLAR) AND ZNCL2 (0.02 MILLIMOLAR)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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