1j53: Difference between revisions

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New page: left|200px<br /><applet load="1j53" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j53, resolution 1.8Å" /> '''Structure of the N-te...
 
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[[Image:1j53.gif|left|200px]]<br /><applet load="1j53" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1j53.gif|left|200px]]<br /><applet load="1j53" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1j53, resolution 1.8&Aring;" />
caption="1j53, resolution 1.8&Aring;" />
'''Structure of the N-terminal Exonuclease Domain of the Epsilon Subunit of E.coli DNA Polymerase III at pH 8.5'''<br />
'''Structure of the N-terminal Exonuclease Domain of the Epsilon Subunit of E.coli DNA Polymerase III at pH 8.5'''<br />


==Overview==
==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.
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==
1J53 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=1J53 OCA].  
1J53 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=1J53 OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brown, S.E.]]
[[Category: Brown, S E.]]
[[Category: Carr, P.D.]]
[[Category: Carr, P D.]]
[[Category: Dixon, N.E.]]
[[Category: Dixon, N E.]]
[[Category: Hamdan, S.]]
[[Category: Hamdan, S.]]
[[Category: Ollis, D.L.]]
[[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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