3uxp
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | [[Image:3uxp.jpg|left|200px]] | ||
- | |||
{{STRUCTURE_3uxp| PDB=3uxp | SCENE= }} | {{STRUCTURE_3uxp| PDB=3uxp | SCENE= }} | ||
- | |||
===Co-crystal Structure of Rat DNA polymerase beta Mutator I260Q: Enzyme-DNA-ddTTP=== | ===Co-crystal Structure of Rat DNA polymerase beta Mutator I260Q: Enzyme-DNA-ddTTP=== | ||
+ | {{ABSTRACT_PUBMED_23651085}} | ||
+ | ==Function== | ||
+ | [[http://www.uniprot.org/uniprot/DPOLB_RAT DPOLB_RAT]] 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. | ||
==About this Structure== | ==About this Structure== | ||
[[3uxp]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UXP OCA]. | [[3uxp]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UXP OCA]. | ||
+ | |||
+ | ==See Also== | ||
+ | *[[DNA polymerase|DNA polymerase]] | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:023651085</ref><references group="xtra"/><references/> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Gridley, C L.]] | [[Category: Gridley, C L.]] |
Revision as of 05:54, 28 August 2013
Contents |
Co-crystal Structure of Rat DNA polymerase beta Mutator I260Q: Enzyme-DNA-ddTTP
Template:ABSTRACT PUBMED 23651085
Function
[DPOLB_RAT] 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.
About this Structure
3uxp is a 6 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
See Also
Reference
- Gridley CL, Rangarajan S, Firbank S, Dalal S, Sweasy JB, Jaeger J. Structural changes in the hydrophobic hinge region adversely affect the activity and fidelity of the I260Q mutator DNA polymerase beta. Biochemistry. 2013 Jun 25;52(25):4422-32. doi: 10.1021/bi301368f. Epub 2013 Jun, 12. PMID:23651085 doi:10.1021/bi301368f