2py5: Difference between revisions

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[[Image:2py5.jpg|left|200px]]
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{{STRUCTURE_2py5|  PDB=2py5  |  SCENE=  }}  
{{STRUCTURE_2py5|  PDB=2py5  |  SCENE=  }}  


'''Phi29 DNA polymerase complexed with single-stranded DNA'''
===Phi29 DNA polymerase complexed with single-stranded DNA===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Vega, M de.]]
[[Category: Vega, M de.]]
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
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Revision as of 20:55, 28 July 2008

File:2py5.png

Template:STRUCTURE 2py5

Phi29 DNA polymerase complexed with single-stranded DNA

Template:ABSTRACT PUBMED 17611604

About this Structure

2PY5 is a Single protein structure of sequence from Bacillus phage phi29. 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 25;26(14):3494-505. Epub 2007 Jul 5. PMID:17611604

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