1j54

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(New page: 200px<br /><applet load="1j54" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j54, resolution 1.7&Aring;" /> '''Structure of the N-te...)
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[[Image:1j54.jpg|left|200px]]<br /><applet load="1j54" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1j54, resolution 1.7&Aring;" />
'''Structure of the N-terminal exonuclease domain of the epsilon subunit of E.coli DNA polymerase III at pH 5.8'''<br />
'''Structure of the N-terminal exonuclease domain of the epsilon subunit of E.coli DNA polymerase III at pH 5.8'''<br />
==Overview==
==Overview==
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The epsilon subunit of the Escherichia coli replicative DNA polymerase III, is the proofreading 3'-5' exonuclease. Structures of its catalytic, N-terminal domain (epsilon186) were determined at two pH values (5.8 and, 8.5) at resolutions of 1.7-1.8 A, in complex with two Mn(II) ions and a, nucleotide product of its reaction, thymidine 5'-monophosphate. The, protein structure is built around a core five-stranded beta sheet that is, a common feature of members of the DnaQ superfamily. The structures were, identical, except for differences in the way TMP and water molecules are, coordinated to the binuclear metal center in the active site. These data, are used to develop a mechanism for epsilon and to produce a plausible, model of the complex of epsilon186 with DNA.
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The epsilon subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3'-5' exonuclease. Structures of its catalytic N-terminal domain (epsilon186) were determined at two pH values (5.8 and 8.5) at resolutions of 1.7-1.8 A, in complex with two Mn(II) ions and a nucleotide product of its reaction, thymidine 5'-monophosphate. The protein structure is built around a core five-stranded beta sheet that is a common feature of members of the DnaQ superfamily. The structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site. These data are used to develop a mechanism for epsilon and to produce a plausible model of the complex of epsilon186 with DNA.
==About this Structure==
==About this Structure==
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1J54 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN, TMP 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J54 OCA].
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1J54 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=TMP:'>TMP</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=1J54 OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Brown, S.E.]]
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[[Category: Brown, S E.]]
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[[Category: Carr, P.D.]]
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[[Category: Carr, P D.]]
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[[Category: Dixon, N.E.]]
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[[Category: Dixon, N E.]]
[[Category: Hamdan, S.]]
[[Category: Hamdan, S.]]
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[[Category: Ollis, D.L.]]
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[[Category: Ollis, D L.]]
[[Category: EDO]]
[[Category: EDO]]
[[Category: MN]]
[[Category: MN]]
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[[Category: dna polymerase proofreading domain]]
[[Category: dna polymerase proofreading domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:56:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:00 2008''

Revision as of 11:19, 21 February 2008


1j54, resolution 1.7Å

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Structure of the N-terminal exonuclease domain of the epsilon subunit of E.coli DNA polymerase III at pH 5.8

Overview

The epsilon subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3'-5' exonuclease. Structures of its catalytic N-terminal domain (epsilon186) were determined at two pH values (5.8 and 8.5) at resolutions of 1.7-1.8 A, in complex with two Mn(II) ions and a nucleotide product of its reaction, thymidine 5'-monophosphate. The protein structure is built around a core five-stranded beta sheet that is a common feature of members of the DnaQ superfamily. The structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site. These data are used to develop a mechanism for epsilon and to produce a plausible model of the complex of epsilon186 with DNA.

About this Structure

1J54 is a Single protein structure of sequence from 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

Structural basis for proofreading during replication of the Escherichia coli chromosome., Hamdan S, Carr PD, Brown SE, Ollis DL, Dixon NE, Structure. 2002 Apr;10(4):535-46. PMID:11937058

Page seeded by OCA on Thu Feb 21 13:19:00 2008

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