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1qrr

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(New page: 200px<br /><applet load="1qrr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qrr, resolution 1.6&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1qrr.gif|left|200px]]<br /><applet load="1qrr" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qrr.gif|left|200px]]<br /><applet load="1qrr" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qrr, resolution 1.6&Aring;" />
caption="1qrr, resolution 1.6&Aring;" />
'''CRYSTAL STRUCTURE OF SQD1 PROTEIN COMPLEX WITH NAD AND UDP-GLUCOSE'''<br />
'''CRYSTAL STRUCTURE OF SQD1 PROTEIN COMPLEX WITH NAD AND UDP-GLUCOSE'''<br />
==Overview==
==Overview==
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The SQD1 enzyme is believed to be involved in the biosynthesis of the, sulfoquinovosyl headgroup of plant sulfolipids, catalyzing the transfer of, SO(3)(-) to UDP-glucose. We have determined the structure of the complex, of SQD1 from Arabidopsis thaliana with NAD(+) and the putative substrate, UDP-glucose at 1.6-A resolution. Both bound ligands are completely buried, within the binding cleft, along with an internal solvent cavity which is, the likely binding site for the, as yet, unidentified sulfur-donor, substrate. SQD1 is a member of the short-chain dehydrogenase/reductase, (SDR) family of enzymes, and its structure shows a conservation of the SDR, catalytic residues. Among several highly conserved catalytic residues, Thr-145 forms unusually short hydrogen bonds with both susceptible, hydroxyls of UDP-glucose. A His side chain may also be catalytically, important in the sulfonation.
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The SQD1 enzyme is believed to be involved in the biosynthesis of the sulfoquinovosyl headgroup of plant sulfolipids, catalyzing the transfer of SO(3)(-) to UDP-glucose. We have determined the structure of the complex of SQD1 from Arabidopsis thaliana with NAD(+) and the putative substrate UDP-glucose at 1.6-A resolution. Both bound ligands are completely buried within the binding cleft, along with an internal solvent cavity which is the likely binding site for the, as yet, unidentified sulfur-donor substrate. SQD1 is a member of the short-chain dehydrogenase/reductase (SDR) family of enzymes, and its structure shows a conservation of the SDR catalytic residues. Among several highly conserved catalytic residues, Thr-145 forms unusually short hydrogen bonds with both susceptible hydroxyls of UDP-glucose. A His side chain may also be catalytically important in the sulfonation.
==About this Structure==
==About this Structure==
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1QRR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with SO4, NAD and UPG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QRR OCA].
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1QRR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=UPG:'>UPG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QRR OCA].
==Reference==
==Reference==
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[[Category: Benning, C.]]
[[Category: Benning, C.]]
[[Category: Essigmann, B.]]
[[Category: Essigmann, B.]]
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[[Category: Garavito, R.M.]]
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[[Category: Garavito, R M.]]
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[[Category: Mulichak, A.M.]]
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[[Category: Mulichak, A M.]]
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[[Category: Theisen, M.J.]]
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[[Category: Theisen, M J.]]
[[Category: NAD]]
[[Category: NAD]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: short hydrogen bonds]]
[[Category: short hydrogen bonds]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:55:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:57 2008''

Revision as of 12:43, 21 February 2008


1qrr, resolution 1.6Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF SQD1 PROTEIN COMPLEX WITH NAD AND UDP-GLUCOSE

Overview

The SQD1 enzyme is believed to be involved in the biosynthesis of the sulfoquinovosyl headgroup of plant sulfolipids, catalyzing the transfer of SO(3)(-) to UDP-glucose. We have determined the structure of the complex of SQD1 from Arabidopsis thaliana with NAD(+) and the putative substrate UDP-glucose at 1.6-A resolution. Both bound ligands are completely buried within the binding cleft, along with an internal solvent cavity which is the likely binding site for the, as yet, unidentified sulfur-donor substrate. SQD1 is a member of the short-chain dehydrogenase/reductase (SDR) family of enzymes, and its structure shows a conservation of the SDR catalytic residues. Among several highly conserved catalytic residues, Thr-145 forms unusually short hydrogen bonds with both susceptible hydroxyls of UDP-glucose. A His side chain may also be catalytically important in the sulfonation.

About this Structure

1QRR is a Single protein structure of sequence from Arabidopsis thaliana with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose., Mulichak AM, Theisen MJ, Essigmann B, Benning C, Garavito RM, Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13097-102. PMID:10557279

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