4ymm: Difference between revisions

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'''Unreleased structure'''


The entry 4ymm is ON HOLD  until Paper Publication
==Structure of human DNA polymerase beta complexed with 7BG as the template base in a 1-nucleotide gapped DNA==
 
<StructureSection load='4ymm' size='340' side='right' caption='[[4ymm]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
Authors: Lee, S., Koag, M.-C.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4ymm]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YMM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YMM FirstGlance]. <br>
Description: Structure of human DNA polymerase beta complexed with 7BG as the template base in a 1-nucleotide gapped DNA
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=7BG:2-AMINO-7-BENZYL-9-(2-DEOXY-2-FLUORO-5-O-PHOSPHONO-BETA-D-ARABINOFURANOSYL)-6-OXO-6,9-DIHYDRO-1H-PURIN-7-IUM'>7BG</scene></td></tr>
[[Category: Koag, M.-C]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ymn|4ymn]], [[4ymo|4ymo]], [[4yn4|4yn4]]</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=4ymm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ymm OCA], [http://pdbe.org/4ymm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ymm RCSB], [http://www.ebi.ac.uk/pdbsum/4ymm 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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Koag, M C]]
[[Category: Lee, S]]
[[Category: Lee, S]]
[[Category: Dna polymerase]]
[[Category: Transferase-dna complex]]

Revision as of 06:50, 10 March 2016

Structure of human DNA polymerase beta complexed with 7BG as the template base in a 1-nucleotide gapped DNAStructure of human DNA polymerase beta complexed with 7BG as the template base in a 1-nucleotide gapped DNA

Structural highlights

4ymm is a 4 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

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]

References

  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

4ymm, resolution 2.20Å

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OCA