1QRR

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

1QRR の概要

• エントリーDOI: 10.2210/pdb1qrr/pdb
• 分子名称: sulfolipid biosynthesis (SQD1) PROTEIN, SULFATE ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: rossmann fold, short hydrogen bonds, sdr homolog, isomerase
• 由来する生物種: Arabidopsis thaliana (thale cress)
• 細胞内の位置: Plastid, chloroplast : O48917
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45786.24

構造登録者

Mulichak, A.M.,Theisen, M.J.,Essigmann, B.,Benning, C.,Garavito, R.M. (登録日: 1999-06-15, 公開日: 1999-11-10, 最終更新日: 2024-02-14)

主引用文献

Mulichak, A.M.,Theisen, M.J.,Essigmann, B.,Benning, C.,Garavito, R.M.
Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose.
Proc.Natl.Acad.Sci.USA, 96:13097-13102, 1999

PubMed Abstract: 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.

PubMed: 10557279
DOI: 10.1073/pnas.96.23.13097

実験手法

X-RAY DIFFRACTION (1.6 Å)