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Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose

by Benning, C , Theisen, M.J , Essigmann, B , Mulichak, A.M , Garavito, R.M

in analogs & derivatives / Arabidopsis Proteins / Arabidopsis thaliana / Atomic interactions / Atoms / Binding Sites / Biochemistry / Biological Sciences / Biosynthesis / chemistry / Crystallography, X-Ray / crystals / Enzymes / Enzymes - chemistry / Enzymes - metabolism / enzymology / Flowers & plants / Glucose / Hydrogen bonds / Hydroxyls / ligands / metabolism / Models, Molecular / molecular conformation / Molecules / NAD / NAD (coenzyme) / NAD - metabolism / NADP / NADP - metabolism / oxidoreductases / Oxygen / pdb/1qrr / phosphates / phosphates (esters) / Plant Proteins / Plant Proteins - chemistry / Plant Proteins - metabolism / Plants / Plants - enzymology / Plants - metabolism / Protein Conformation / Proteins / Sulfur / udp-glucose / Uridine Diphosphate Glucose / Uridine Diphosphate Glucose - analogs & derivatives / Uridine Diphosphate Glucose - biosynthesis / Uridine Diphosphate Glucose - metabolism / X-ray diffraction

1999

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Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose

by Benning, C , Theisen, M.J , Essigmann, B , Mulichak, A.M , Garavito, R.M

1999

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Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose

by Benning, C , Theisen, M.J , Essigmann, B , Mulichak, A.M , Garavito, R.M

1999

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Journal Article

Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose

Benning, C,

Theisen, M.J,

Essigmann, B,

Mulichak, A.M,

Garavito, R.M

1999

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-angstrom 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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Publisher

National Academy of Sciences of the United States of America,National Acad Sciences,National Academy of Sciences,The National Academy of Sciences

Subject

analogs & derivatives

/ Arabidopsis Proteins

/ Arabidopsis thaliana

/ Atomic interactions

/ Atoms

/ Binding Sites

/ Biochemistry