1t7p

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(New page: 200px<br /><applet load="1t7p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t7p, resolution 2.2&Aring;" /> '''T7 DNA POLYMERASE COM...)
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[[Image:1t7p.gif|left|200px]]<br /><applet load="1t7p" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1t7p.gif|left|200px]]<br /><applet load="1t7p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1t7p, resolution 2.2&Aring;" />
caption="1t7p, resolution 2.2&Aring;" />
'''T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN'''<br />
'''T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN'''<br />
==Overview==
==Overview==
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DNA polymerases change their specificity for nucleotide substrates with, each catalytic cycle, while achieving error frequencies in the range of, 10(-5) to 10(-6). Here we present a 2.2 A crystal structure of the, replicative DNA polymerase from bacteriophage T7 complexed with a, primer-template and a nucleoside triphosphate in the polymerase active, site. The structure illustrates how nucleotides are selected in a, template-directed manner, and provides a structural basis for a, metal-assisted mechanism of phosphoryl transfer by a large group of, related polymerases.
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DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10(-5) to 10(-6). Here we present a 2.2 A crystal structure of the replicative DNA polymerase from bacteriophage T7 complexed with a primer-template and a nucleoside triphosphate in the polymerase active site. The structure illustrates how nucleotides are selected in a template-directed manner, and provides a structural basis for a metal-assisted mechanism of phosphoryl transfer by a large group of related polymerases.
==About this Structure==
==About this Structure==
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1T7P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG and DG3 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T7P OCA].
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1T7P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=DG3:'>DG3</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=1T7P OCA].
==Reference==
==Reference==
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[[Category: Doublie, S.]]
[[Category: Doublie, S.]]
[[Category: Ellenberger, T.]]
[[Category: Ellenberger, T.]]
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[[Category: Long, A.M.]]
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[[Category: Long, A M.]]
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[[Category: Richardson, C.C.]]
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[[Category: Richardson, C C.]]
[[Category: Tabor, S.]]
[[Category: Tabor, S.]]
[[Category: DG3]]
[[Category: DG3]]
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[[Category: thioredoxin]]
[[Category: thioredoxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:03:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:45 2008''

Revision as of 13:10, 21 February 2008


1t7p, resolution 2.2Å

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T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN

Overview

DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10(-5) to 10(-6). Here we present a 2.2 A crystal structure of the replicative DNA polymerase from bacteriophage T7 complexed with a primer-template and a nucleoside triphosphate in the polymerase active site. The structure illustrates how nucleotides are selected in a template-directed manner, and provides a structural basis for a metal-assisted mechanism of phosphoryl transfer by a large group of related polymerases.

About this Structure

1T7P is a Protein complex structure of sequences from Bacteriophage t7 and Escherichia coli 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

Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution., Doublie S, Tabor S, Long AM, Richardson CC, Ellenberger T, Nature. 1998 Jan 15;391(6664):251-8. PMID:9440688

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