4mfc: Difference between revisions
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{{STRUCTURE_4mfc| PDB=4mfc | SCENE= }} | |||
===Structure of human DNA polymerase beta complexed with O6MG in the template base paired with incoming non-hydrolyzable CTP=== | |||
{{ABSTRACT_PUBMED_24694247}} | |||
==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> | |||
==About this Structure== | |||
[[4mfc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MFC OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024694247</ref><references group="xtra"/><references/> | |||
[[Category: Koag, M C.]] | |||
[[Category: Lee, S.]] | |||
[[Category: Min, K.]] | |||
[[Category: Monzingo, A F.]] | |||
[[Category: Dna polymerase x family]] | |||
[[Category: Dna synthesis]] | |||
[[Category: Transferase-dna complex]] | |||
Revision as of 12:52, 16 April 2014
Structure of human DNA polymerase beta complexed with O6MG in the template base paired with incoming non-hydrolyzable CTPStructure of human DNA polymerase beta complexed with O6MG in the template base paired with incoming non-hydrolyzable CTP
Template:ABSTRACT PUBMED 24694247
FunctionFunction
[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 StructureAbout this Structure
4mfc is a 4 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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
- ↑ 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