6IWK

The Structure of Maltooligosaccharide-forming Amylase from Pseudomonas saccharophila STB07

6IWK の概要

• エントリーDOI: 10.2210/pdb6iwk/pdb
• 分子名称: Glucan 1,4-alpha-maltotetraohydrolase, GLYCEROL, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: maltooligosaccharide-forming amylas, pseudomonas saccharophila stb07, sugar binding protein
• 由来する生物種: Pelomonas saccharophila (Pseudomonas saccharophila)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46588.93

構造登録者

Li, Z.F.,Ban, X.F.,Zhang, Z.Q.,Li, C.M.,Gu, Z.B.,Jin, T.C.,Li, Y.L.,Shang, Y.H. (登録日: 2018-12-05, 公開日: 2019-12-11, 最終更新日: 2024-11-20)

主引用文献

Zhang, Z.,Jin, T.,Xie, X.,Ban, X.,Li, C.,Hong, Y.,Cheng, L.,Gu, Z.,Li, Z.
Structure of maltotetraose-forming amylase from Pseudomonas saccharophila STB07 provides insights into its product specificity.
Int.J.Biol.Macromol., 154:1303-1313, 2020

PubMed Abstract: The maltooligosaccharide-forming amylases (MFAses) degrade starch into maltooligosaccharides which potentially benefit human diet and grow popular in food processing, but little has been studied about their product specificity and structures. We focused on this topic and provide evidence through an X-ray crystal structure of the maltotetraose (G4)-forming amylase from Pseudomonas saccharophila STB07 (MFA), as well as co-crystal structures of MFA with G4 and with pseudo-maltoheptaose (pseudo-G7) determined at up to 1.1 Å resolution. G4 and pseudo-G7 occupy active cleft subsites -4 to -1 and -4 to +3 respectively. Binding induces conformational changes in the active sites except Asp193, working as the base catalyst. Comparison of the MFA structure with those of other α-amylases revealed obvious differences in the loop structures providing dominant interactions between protein and substrate in the non-reducing side of the active sites cleft. These structures at the non-reducing end may govern the G4 specificity of MFA and also be relevant to its exo-type action pattern.

PubMed: 31751711
DOI: 10.1016/j.ijbiomac.2019.11.006

実験手法

X-RAY DIFFRACTION (1.501 Å)