1QHP

FIVE-DOMAIN ALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE COMPLEX

1QHP の概要

• エントリーDOI: 10.2210/pdb1qhp/pdb
• 関連するPDBエントリー: 1QHO
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: ALPHA-AMYLASE, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: amylase, glycoside hydrolase, starch degradation, hydrolase
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 76800.30

構造登録者

Dauter, Z.,Dauter, M.,Brzozowski, A.M.,Christensen, S.,Borchert, T.V.,Beier, L.,Wilson, K.S.,Davies, G.J. (登録日: 1999-05-25, 公開日: 2000-05-31, 最終更新日: 2023-09-20)

主引用文献

Dauter, Z.,Dauter, M.,Brzozowski, A.M.,Christensen, S.,Borchert, T.V.,Beier, L.,Wilson, K.S.,Davies, G.J.
X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.
Biochemistry, 38:8385-8392, 1999

PubMed Abstract: The three-dimensional structure of the Bacillus stearothermophilus "maltogenic" alpha-amylase, Novamyl, has been determined by X-ray crystallography at a resolution of 1.7 A. Unlike conventional alpha-amylases from glycoside hydrolase family 13, Novamyl exhibits the five-domain structure more usually associated with cyclodextrin glycosyltransferase. Complexes of the enzyme with both maltose and the inhibitor acarbose have been characterized. In the maltose complex, two molecules of maltose are found in the -1 to -2 and +2 to +3 subsites of the active site, with two more on the C and E domains. The C-domain maltose occupies a position identical to one previously observed in the Bacillus circulans CGTase structure [Lawson, C. L., et al. (1994) J. Mol. Biol. 236, 590-600], suggesting that the C-domain plays a genuine biological role in saccharide binding. In the acarbose-maltose complex, the tetrasaccharide inhibitor acarbose is found as an extended hexasaccharide species, bound in the -3 to +3 subsites. The transition state mimicking pseudosaccharide is bound in the -1 subsite of the enzyme in a 2H3 half-chair conformation, as expected. The active site of Novamyl lies in an open gully, fully consistent with its ability to perform internal cleavage via an endo as opposed to an exo activity.

PubMed: 10387084
DOI: 10.1021/bi990256l

実験手法

X-RAY DIFFRACTION (1.7 Å)