2pyl
From Proteopedia
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Phi29 DNA polymerase complexed with primer-template DNA and incoming nucleotide substrates (ternary complex)
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
2PYL is a Single protein structure of sequence from Vibrio phage f237 with MG, TTP and EDO as ligands. 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
Page seeded by OCA on Wed Nov 21 13:44:12 2007
