1S97

DPO4 with GT mismatch

Summary for 1S97

• Entry DOI: 10.2210/pdb1s97/pdb
• Descriptor: 5'-D(*GP*GP*GP*GP*GP*AP*AP*GP*GP*AP*CP*TP*G)-3', 5'-D(*T*TP*CP*AP*GP*TP*AP*GP*TP*CP*CP*TP*TP*CP*CP*CP*CP*C)-3', DNA polymerase IV, ... (6 entities in total)
• Functional Keywords: protein-dna complex, dna duplex, g.t mismatch, transferase-dna complex, transferase/dna
• Biological source: Sulfolobus solfataricus
• Cellular location: Cytoplasm (Probable): Q97W02
• Total number of polymer chains: 12
• Total formula weight: 200997.11

Authors

Trincao, J.,Johnson, R.E.,Wolfle, W.T.,Escalante, C.R.,Prakash, S.,Prakash, L.,Aggarwal, A.K. (deposition date: 2004-02-03, release date: 2004-04-27, Last modification date: 2023-08-23)

Primary citation

Trincao, J.,Johnson, R.E.,Wolfle, W.T.,Escalante, C.R.,Prakash, S.,Prakash, L.,Aggarwal, A.K.
Dpo4 is hindered in extending a G.T mismatch by a reverse wobble
Nat.Struct.Mol.Biol., 11:457-462, 2004

PubMed Abstract: 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.

PubMed: 15077104
DOI: 10.1038/nsmb755

Experimental method

X-RAY DIFFRACTION (2.4 Å)