6XSJ

X-ray structure of a monoclinic form of alpha amylase from Aspergillus at 1.4 A resolution

6XSJ の概要

• エントリーDOI: 10.2210/pdb6xsj/pdb
• 分子名称: Alpha-amylase, alpha-D-mannopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (10 entities in total)
• 機能のキーワード: substrate complex, homology, catalytic site, novo enzyme, sugar binding protein
• 由来する生物種: Aspergillus oryzae (Yellow koji mold)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 111215.05

構造登録者

McPherson, A. (登録日: 2020-07-15, 公開日: 2020-10-14, 最終更新日: 2024-10-30)

主引用文献

Gee, C.L.,Holton, J.M.,McPherson, A.
Structures of two novel crystal forms of Aspergillus oryzae alpha amylase (taka-amylase).
J.Biosci.Bioeng., 131:605-612, 2021

PubMed Abstract: The structures of Aspergillus oryzae α-amylase were determined in a tetragonal crystal, having one molecule as asymmetric unit, and a monoclinic crystal with two molecules as asymmetric unit. Both crystal forms were obtained from trace contaminants of an old commercial lipase preparation. Structures were determined and refined to 1.65 Å and 1.43 Å resolution respectively. The latter crystal has a non-crystallographic (NCS) twofold axis within the asymmetric unit. Glycosylation at Asn197 is evident, and in the tetragonal crystal can be seen to include three, partially disordered sugar residues following the initial N-acetyl glucosamine (NAG). Superposition of the tetragonal crystal model on the α-amylases from Bacillus subtilis (PDB:1BAG), pig pancreas (PDB:3L2L), and barley (PDB:1AMY), show a high degree of coincidence, particularly for the (β/α)-barrel domains, and especially within the active site. Using this structural agreement between amylases, we extrapolated the binding model of a six residue, limit dextrin found in pig pancreas α-amylase to the A. oryzae enzyme model, which predicts substrate interacting amino acid residues.

PubMed: 33814275
DOI: 10.1016/j.jbiosc.2021.02.008

実験手法

X-RAY DIFFRACTION (1.4 Å)