3uxp

Co-crystal Structure of Rat DNA polymerase beta Mutator I260Q: Enzyme-DNA-ddTTPCo-crystal Structure of Rat DNA polymerase beta Mutator I260Q: Enzyme-DNA-ddTTP

FunctionFunction

[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 StructureAbout this Structure

3uxp is a 6 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ 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

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OCA

[1] 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

[xtra 1]