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| [[Image:1qrr.gif|left|200px]] | | {{Seed}} |
| | [[Image:1qrr.png|left|200px]] |
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| {{STRUCTURE_1qrr| PDB=1qrr | SCENE= }} | | {{STRUCTURE_1qrr| PDB=1qrr | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF SQD1 PROTEIN COMPLEX WITH NAD AND UDP-GLUCOSE'''
| | ===CRYSTAL STRUCTURE OF SQD1 PROTEIN COMPLEX WITH NAD AND UDP-GLUCOSE=== |
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| ==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. | | The line below this paragraph, {{ABSTRACT_PUBMED_10557279}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10557279 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10557279}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Sdr homolog]] | | [[Category: Sdr homolog]] |
| [[Category: Short hydrogen bond]] | | [[Category: Short hydrogen bond]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:37:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:22:55 2008'' |