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2py5
From Proteopedia
(New page: 200px<br /><applet load="2py5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2py5, resolution 1.60Å" /> '''Phi29 DNA polymerase...) |
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| - | [[Image:2py5.jpg|left|200px]]<br /><applet load="2py5" size=" | + | [[Image:2py5.jpg|left|200px]]<br /><applet load="2py5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2py5, resolution 1.60Å" /> | caption="2py5, resolution 1.60Å" /> | ||
'''Phi29 DNA polymerase complexed with single-stranded DNA'''<br /> | '''Phi29 DNA polymerase complexed with single-stranded DNA'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PY5 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 EDO as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 2PY5 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=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2PY5 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 14:14:46 2008'' |
Revision as of 12:14, 23 January 2008
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Phi29 DNA polymerase complexed with single-stranded DNA
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 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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