2py5
Phi29 DNA polymerase complexed with single-stranded DNA
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Overview
Replicative DNA polymerases (DNAPs) move along template DNA in a, processive manner. The structural basis of the mechanism of translocation, has been better studied in the A-family of polymerases than in the, B-family of replicative polymerases. To address this issue, we have, determined the X-ray crystal structures of phi29 DNAP, a member of the, protein-primed subgroup of the B-family of polymerases, complexed with, primer-template DNA in the presence or absence of the incoming nucleoside, triphosphate, the pre- and post-translocated states, respectively., Comparison of these structures reveals a mechanism of translocation that, appears to be facilitated by the coordinated movement of two conserved, tyrosine residues into the insertion site. This differs from the mechanism, employed by the A-family polymerases, in which a conserved tyrosine moves, into the templating and insertion sites during the translocation step., Polymerases from the two families also interact with downstream, single-stranded template DNA in very different ways.
About this Structure
2PY5 is a Single protein structure of sequence from Vibrio phage f237 with EDO as ligand. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases., Berman AJ, Kamtekar S, Goodman JL, Lazaro JM, de Vega M, Blanco L, Salas M, Steitz TA, EMBO J. 2007 Jul 5;. PMID:17611604
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