2pyl
From Proteopedia
(New page: 200px<br /><applet load="2pyl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pyl, resolution 2.20Å" /> '''Phi29 DNA polymerase...) |
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| - | [[Image:2pyl.gif|left|200px]]<br /><applet load="2pyl" size=" | + | [[Image:2pyl.gif|left|200px]]<br /><applet load="2pyl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2pyl, resolution 2.20Å" /> | caption="2pyl, resolution 2.20Å" /> | ||
'''Phi29 DNA polymerase complexed with primer-template DNA and incoming nucleotide substrates (ternary complex)'''<br /> | '''Phi29 DNA polymerase complexed with primer-template DNA and incoming nucleotide substrates (ternary complex)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237] with MG, TTP and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http:// | + | 2PYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=TTP:'>TTP</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PYL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:14:48 2008'' |
Revision as of 12:14, 23 January 2008
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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 , and 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
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