1qor

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(New page: 200px<br /><applet load="1qor" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qor, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1qor.gif|left|200px]]<br /><applet load="1qor" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qor.gif|left|200px]]<br /><applet load="1qor" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qor, resolution 2.2&Aring;" />
caption="1qor, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURE OF ESCHERICHIA COLI QUINONE OXIDOREDUCTASE COMPLEXED WITH NADPH'''<br />
'''CRYSTAL STRUCTURE OF ESCHERICHIA COLI QUINONE OXIDOREDUCTASE COMPLEXED WITH NADPH'''<br />
==Overview==
==Overview==
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The crystal structure of the homodimer of quinone oxidoreductase from, Escherichia coli has been determined using the multiple isomorphous, replacement method at 2.2 A resolution and refined to an R-factor of 14.1%, The crystallographic asymmetric unit contains one functional dimer with, the two subunits being related by a non-crystallographic 2-fold symmetry, axis. The model consists of two polypeptide chains (residues 2 through, 327), one NADPH molecule and one sulphate anion per subunit, and 432 water, molecules. Each subunit consists of two domains: a catalytic domain and a, nucleotide-binding domain with the NADPH co-factor bound in the cleft, between domains. Quinone oxidoreductase has an unusual nucleotide-binding, fingerprint motif consisting of the sequence AXXGXXG. The overall, structure of quinone oxidoreductase shows strong structural homology to, that of horse liver alcohol dehydrogenase.
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The crystal structure of the homodimer of quinone oxidoreductase from Escherichia coli has been determined using the multiple isomorphous replacement method at 2.2 A resolution and refined to an R-factor of 14.1% The crystallographic asymmetric unit contains one functional dimer with the two subunits being related by a non-crystallographic 2-fold symmetry axis. The model consists of two polypeptide chains (residues 2 through 327), one NADPH molecule and one sulphate anion per subunit, and 432 water molecules. Each subunit consists of two domains: a catalytic domain and a nucleotide-binding domain with the NADPH co-factor bound in the cleft between domains. Quinone oxidoreductase has an unusual nucleotide-binding fingerprint motif consisting of the sequence AXXGXXG. The overall structure of quinone oxidoreductase shows strong structural homology to that of horse liver alcohol dehydrogenase.
==About this Structure==
==About this Structure==
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1QOR 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 SO4 and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QOR OCA].
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1QOR 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=SO4:'>SO4</scene> and <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOR OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Barton, J.D.]]
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[[Category: Barton, J D.]]
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[[Category: Dixon, N.E.]]
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[[Category: Dixon, N E.]]
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[[Category: Edwards, K.J.]]
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[[Category: Edwards, K J.]]
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[[Category: Ollis, D.L.]]
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[[Category: Ollis, D L.]]
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[[Category: Thorn, J.M.]]
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[[Category: Thorn, J M.]]
[[Category: NAP]]
[[Category: NAP]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:51:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:04 2008''

Revision as of 12:42, 21 February 2008


1qor, resolution 2.2Å

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CRYSTAL STRUCTURE OF ESCHERICHIA COLI QUINONE OXIDOREDUCTASE COMPLEXED WITH NADPH

Overview

The crystal structure of the homodimer of quinone oxidoreductase from Escherichia coli has been determined using the multiple isomorphous replacement method at 2.2 A resolution and refined to an R-factor of 14.1% The crystallographic asymmetric unit contains one functional dimer with the two subunits being related by a non-crystallographic 2-fold symmetry axis. The model consists of two polypeptide chains (residues 2 through 327), one NADPH molecule and one sulphate anion per subunit, and 432 water molecules. Each subunit consists of two domains: a catalytic domain and a nucleotide-binding domain with the NADPH co-factor bound in the cleft between domains. Quinone oxidoreductase has an unusual nucleotide-binding fingerprint motif consisting of the sequence AXXGXXG. The overall structure of quinone oxidoreductase shows strong structural homology to that of horse liver alcohol dehydrogenase.

About this Structure

1QOR is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH., Thorn JM, Barton JD, Dixon NE, Ollis DL, Edwards KJ, J Mol Biol. 1995 Jun 16;249(4):785-99. PMID:7602590

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