3VM7

Structure of an Alpha-Amylase from Malbranchea cinnamomea

3VM7 の概要

• エントリーDOI: 10.2210/pdb3vm7/pdb
• 分子名称: Alpha-amylase, CALCIUM ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: malbranchea cinnamomea c -amylase cmodels, protein conformation, hydrolase
• 由来する生物種: Malbranchea cinnamomea
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54595.87

構造登録者

Zhou, P.,Hu, S.Q.,Zhou, Y.,Han, P.,Yang, S.Q.,Jiang, Z.Q. (登録日: 2011-12-09, 公開日: 2013-05-29, 最終更新日: 2024-11-20)

主引用文献

Han, P.,Zhou, P.,Hu, S.,Yang, S.,Yan, Q.,Jiang, Z.Q.
A Novel Multifunctional alpha-Amylase from the Thermophilic Fungus Malbranchea cinnamomea: Biochemical Characterization and Three-Dimensional Structure.
Appl Biochem Biotechnol., 170:420-435, 2013

PubMed Abstract: A novel α-amylase (McAmyA) from the thermophilic fungus, Malbranchea cinnamomea was purified, characterized and crystallized in the present study. McAmyA was purified to apparent homogeneity with a molecular mass of 60.3 kDa on SDS-PAGE. The enzyme exhibited maximal activity at pH 6.5 and was stable within pH 5.0-10.0. It was most active at 65 °C and was stable up to 50 °C. McAmyA was capable of hydrolyzing amylose, starch, amylopectin, pullulan, cyclodextrins and maltooligosaccharides. The full-length cDNA of an α-amylase gene (McAmyA) from the strain was cloned. McAmyA consisted of a 1,476-bp open reading frame encoding 492 amino acids. It displayed the highest amino acid sequence homology (less than 60 %) with the reported α-amylases. The crystal structure of McAmyA was solved at a resolution of 2.25 Å (PDB code 3VM7). The overall structure of McAmyA reveals three domains with ten α helices and 14 β strands, and the putative catalytic residues are positioned at domain A with somewhat different secondary structural circumstances compared with typical α-amylases.

PubMed: 23536251
DOI: 10.1007/s12010-013-0198-y

実験手法

X-RAY DIFFRACTION (2.25 Å)