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1s97
From Proteopedia
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DPO4 with GT mismatch
Overview
The ability or inability of a DNA polymerase to extend a mispair directly, affects the establishment of genomic mutations. We report here kinetic, analyses of the ability of Dpo4, a Y-family polymerase from Sulfolobus, solfataricus, to extend from all mispairs opposite a template G or T. Dpo4, is equally inefficient at extending these mispairs, which include, surprisingly, a G.T mispair expected to conform closely to Watson-Crick, geometry. To elucidate the basis of this, we solved the structure of Dpo4, bound to G.T-mispaired primer template in the presence of an incoming, nucleotide. As a control, we also determined the structure of Dpo4 bound, to a matched A-T base pair at the primer terminus. The structures offer a, basis for the low efficiency of Dpo4 in extending a G.T mispair: a reverse, wobble that deflects the primer 3'-OH away from the incoming nucleotide.
About this Structure
1S97 is a Single protein structure of sequence from Sulfolobus solfataricus with CA and DCT as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Dpo4 is hindered in extending a G.T mismatch by a reverse wobble., Trincao J, Johnson RE, Wolfle WT, Escalante CR, Prakash S, Prakash L, Aggarwal AK, Nat Struct Mol Biol. 2004 May;11(5):457-62. Epub 2004 Apr 11. PMID:15077104
Page seeded by OCA on Wed Nov 21 02:12:39 2007
