1OBF

The crystal structure of Glyceraldehyde 3-phosphate Dehydrogenase from Alcaligenes xylosoxidans at 1.7A resolution.

1OBF の概要

• エントリーDOI: 10.2210/pdb1obf/pdb
• 分子名称: GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE, SULFATE ION, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: glycolytic pathway, oxidoreductase, free-nad gapdh
• 由来する生物種: ACHROMOBACTER XYLOSOXIDANS (ALCALIGENES XYLOSOXIDANS)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72217.49

構造登録者

Antonyuk, S.V.,Eady, R.R.,Strange, R.W.,Hasnain, S.S. (登録日: 2003-01-30, 公開日: 2003-06-12, 最終更新日: 2023-12-13)

主引用文献

Antonyuk, S.V.,Eady, R.R.,Strange, R.W.,Hasnain, S.S.
The Structure of Glyceraldehyde 3-Phosphate Dehydrogenase from Alcaligenes Xylosoxidans at 1.7 A Resolution
Acta Crystallogr.,Sect.D, 59:835-, 2003

PubMed Abstract: The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the Gram-negative denitrifying bacterial species Alcaligenes xylosoxidans was purified and crystallized as a contaminant protein during purification of nitrous oxide reductase. This is the first structure of a GAPDH from a denitrifying species. The crystal structure was solved at 1.7 A resolution by molecular replacement using the structure of GAPDH from Bacillus stearothermophilus as a starting model. The quality of the structure enabled the amino-acid sequence of the A. xylosoxidans GAPDH to be assigned. The structure is that of the apo-enzyme, lacking the NAD+ cofactor and with the active-site residue Cys154 oxidized. The global structure of the enzyme has a homotetrameric quaternary structure similar to that observed for its bacterial and eukaryotic counterparts. The essential role of Cys154 in the enzyme activity has been confirmed. In monomer O two half-occupancy sulfate ions were found at the active site, which are analogous to the substrate and the "attacking" phosphate seen in B. stearothermophilus. One half-occupancy sulfate ion is also located in the substrate-binding site of monomer P.

PubMed: 12777799
DOI: 10.1107/S0907444903041441

実験手法

X-RAY DIFFRACTION (1.7 Å)