4mfc

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'''Unreleased structure'''
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{{STRUCTURE_4mfc| PDB=4mfc | SCENE= }}
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===Structure of human DNA polymerase beta complexed with O6MG in the template base paired with incoming non-hydrolyzable CTP===
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{{ABSTRACT_PUBMED_24694247}}
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The entry 4mfc is ON HOLD until Paper Publication
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==Function==
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[[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>
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Authors: Koag, M.C., Min, K., Monzingo, A.F., Lee, S.
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==About this Structure==
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[[4mfc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MFC OCA].
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Description: Structure of human DNA polymerase beta complexed with O6MG in the template base paired with incoming non-hydrolyzable CTP
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==Reference==
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<ref group="xtra">PMID:024694247</ref><references group="xtra"/><references/>
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[[Category: Koag, M C.]]
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[[Category: Lee, S.]]
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[[Category: Min, K.]]
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[[Category: Monzingo, A F.]]
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[[Category: Dna polymerase x family]]
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[[Category: Dna synthesis]]
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[[Category: Transferase-dna complex]]

Revision as of 09:52, 16 April 2014

Template:STRUCTURE 4mfc

Contents

Structure of human DNA polymerase beta complexed with O6MG in the template base paired with incoming non-hydrolyzable CTP

Template:ABSTRACT PUBMED 24694247

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]

About this Structure

4mfc is a 4 chain structure. Full crystallographic information is available from OCA.

Reference

  • Koag MC, Lee S. Metal-Dependent Conformational Activation Explains Highly Promutagenic Replication across O6-Methylguanine by Human DNA Polymerase beta J Am Chem Soc. 2014 Apr 2. PMID:24694247 doi:http://dx.doi.org/10.1021/ja500172d
  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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

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