1DLI

THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION

1DLI の概要

• エントリーDOI: 10.2210/pdb1dli/pdb
• 関連するPDBエントリー: 1DLJ
• 分子名称: UDP-GLUCOSE DEHYDROGENASE, SULFATE ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: rossmann fold, ternary complex, crystallographic dimer, oxidoreductase
• 由来する生物種: Streptococcus pyogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47301.29

構造登録者

Campbell, R.E.,Mosimann, S.C.,van de Rijn, I.,Tanner, M.E.,Strynadka, N.C.J. (登録日: 1999-12-09, 公開日: 2000-05-31, 最終更新日: 2024-02-07)

主引用文献

Campbell, R.E.,Mosimann, S.C.,van De Rijn, I.,Tanner, M.E.,Strynadka, N.C.
The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation.
Biochemistry, 39:7012-7023, 2000

PubMed Abstract: Bacterial UDP-glucose dehydrogenase (UDPGlcDH) is essential for formation of the antiphagocytic capsule that protects many virulent bacteria such as Streptococcus pyogenes andStreptococcus pneumoniae type 3 from the host's immune system. We have determined the X-ray structures of both native and Cys260Ser UDPGlcDH from S. pyogenes (74% similarity to S. pneumoniae) in ternary complexes with UDP-xylose/NAD(+) and UDP-glucuronic acid/NAD(H), respectively. The 402 residue homodimeric UDPGlcDH is composed of an N-terminal NAD(+) dinucleotide binding domain and a C-terminal UDP-sugar binding domain connected by a long (48 A) central alpha-helix. The first 290 residues of UDPGlcDH share structural homology with 6-phosphogluconate dehydrogenase, including conservation of an active site lysine and asparagine that are implicated in the enzyme mechanism. Also proposed to participate in the catalytic mechanism are a threonine and a glutamate that hydrogen bond to a conserved active site water molecule suitably positioned for general acid/base catalysis.

PubMed: 10841783
DOI: 10.1021/bi000181h

実験手法

X-RAY DIFFRACTION (2.31 Å)