1DOS

STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE

1DOS の概要

• エントリーDOI: 10.2210/pdb1dos/pdb
• 分子名称: ALDOLASE CLASS II, ZINC ION, AMMONIUM ION, ... (4 entities in total)
• 機能のキーワード: lyase, classii fructose 1, 6-bisphosphate aldolase, glycolysis
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78234.73

構造登録者

Blom, N.,Tetreault, S.,Coulombe, R.,Sygusch, J. (登録日: 1996-06-24, 公開日: 1997-07-07, 最終更新日: 2024-02-07)

主引用文献

Blom, N.S.,Tetreault, S.,Coulombe, R.,Sygusch, J.
Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase.
Nat.Struct.Biol., 3:856-862, 1996

PubMed Abstract: The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 A resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barrel carboxyl side of each subunit. In each subunit there are two mutually exclusive zinc metal ion binding sites, 3.2 A apart; the exclusivity is mediated by a conformational transition involving side-chain rotations by chelating histidine residues. A binding site for K+ and NH4+ activators was found near the beta-barrel centre. Although Class I and Class II aldolases catalyse identical reactions, their active sites do not share common amino acid residues, are structurally dissimilar, and from sequence comparisons appear to be evolutionary distinct.

PubMed: 8836102
DOI: 10.1038/nsb1096-856

実験手法

X-RAY DIFFRACTION (1.67 Å)