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2uvw
From Proteopedia
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CRYSTAL STRUCTURES OF MUTANT DPO4 DNA POLYMERASES WITH 8-OXOG CONTAINING DNA TEMPLATE-PRIMER CONSTRUCTS
Overview
Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) has been shown to, catalyze bypass of 7,8-dihydro-8-oxodeoxyguanosine (8-oxoG) in a highly, efficient and relatively accurate manner. Crystal structures have revealed, a potential role for Arg(332) in stabilizing the anti conformation of the, 8-oxoG template base by means of a hydrogen bond or ion-dipole pair, which, results in an increased enzymatic efficiency for dCTP insertion and makes, formation of a Hoogsteen pair between 8-oxoG and dATP less favorable., Site-directed mutagenesis was used to replace Arg(332) with Ala, Glu, Leu, or His in order to probe the importance of Arg(332) in accurate and, efficient bypass of 8-oxoG. The double mutant Ala(331)Ala(332) was also, prepared to address the contribution of Arg(331). Transientstate ... [(full description)]
About this Structure
2UVW is a [Single protein] structure of sequence from [Sulfolobus solfataricus] with CA and DGT as [ligands]. Active as [DNA-directed DNA polymerase], with EC number [2.7.7.7]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Hydrogen bonding of 7,8-dihydro-8-oxodeoxyguanosine with a charged residue in the little finger domain determines miscoding events in Sulfolobus solfataricus DNA polymerase Dpo4., Eoff RL, Irimia A, Angel KC, Egli M, Guengerich FP, J Biol Chem. 2007 Jul 6;282(27):19831-43. Epub 2007 Apr 27. PMID:17468100
Page seeded by OCA on Tue Oct 30 13:10:45 2007
Categories: DNA-directed DNA polymerase | Single protein | Sulfolobus solfataricus | Egli, M. | Irimia, A. | CA | DGT | 7 | 8-dihydro-8-oxodeoxyguanosine | Dna damage | Dna repair | Dna replication | Dna- binding | Dna-binding | Dna-directed dna polymerase | Magnesium | Metal- binding | Metal-binding | Mutator protein | Nucleotidyltransferase | P2 dna polymerase iv | Transferase | Translesion dna polymerase
