2j6t

From Proteopedia

Revision as of 15:21, 30 October 2007

TERNARY COMPLEX OF SULFOLOBUS SOLFATARICUS DPO4 DNA POLYMERASE, O6-METHYLGUANINE MODIFIED DNA, AND DATP.

Overview

We examined the effect of a single O6-methylguanine (O6-MeG) template, residue on catalysis by a model Y family polymerase, Dpo4 from Sulfolobus, solfataricus. Mass spectral analysis of Dpo4-catalyzed extension products, revealed that the enzyme accurately bypasses O6-MeG, with C being the, major product (approximately 70%) and T or A being the minor species, (approximately 20% or approximately 10%, respectively), consistent with, steady-state kinetic parameters. Transient-state kinetic experiments, revealed that kpol, the maximum forward rate constant describing, polymerization, for dCTP incorporation opposite O6-MeG was approximately, 6-fold slower than observed for unmodified G, and no measurable product, was observed for dTTP incorporation in the pre-steady state. The lack of, any ... [(full description)]

About this Structure

2J6T is a [Single protein] structure of sequence from [Sulfolobus solfataricus] with CA and DTP 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

Sulfolobus solfataricus DNA polymerase Dpo4 is partially inhibited by "wobble" pairing between O6-methylguanine and cytosine, but accurate bypass is preferred., Eoff RL, Irimia A, Egli M, Guengerich FP, J Biol Chem. 2007 Jan 12;282(2):1456-67. Epub 2006 Nov 14. PMID:17105728

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