4LPC

Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose

4LPC の概要

• エントリーDOI: 10.2210/pdb4lpc/pdb
• 関連するPDBエントリー: 1M7X 4LQ1
• 関連するBIRD辞書のPRD_ID: PRD_900001 PRD_900009 PRD_900010 PRD_900018
• 分子名称: 1,4-alpha-glucan branching enzyme GlgB, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (9 entities in total)
• 機能のキーワード: branching enzyme, maltoheptaose, linear polysaccharide, starch biosynthetic pathway, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 291366.12

構造登録者

Feng, L.,Geiger, J.H. (登録日: 2013-07-16, 公開日: 2015-04-01, 最終更新日: 2024-02-28)

主引用文献

Feng, L.,Fawaz, R.,Hovde, S.,Gilbert, L.,Chiou, J.,Geiger, J.H.
Crystal Structures of Escherichia coli Branching Enzyme in Complex with Linear Oligosaccharides.
Biochemistry, 54:6207-6218, 2015

PubMed Abstract: Branching enzyme is responsible for all branching of glycogen and starch. It is an unusual member of the α-amylase family because it has both α-1,4-amylase activity and α-1,6-transferase activity [Drummond, G. S., et al. (1972) Eur. J. Biochem. 26, 168-176]. It also does not react with shorter glucans, though it will bind much longer substrates and substrate mimics [Binderup, K., et al. (2002) Arch. Biochem. Biophys. 397, 279-285]. In an effort to better understand how branching enzyme interacts with its polymeric substrate, we have determined the structure of Δ112 Escherichia coli branching enzyme bound to maltoheptaose and maltohexaose. Together, these structures define six distinct oligosaccharide binding sites on the surface of E. coli branching enzyme. Most of these binding sites surround the edge of the β-barrel domain and are quite far from the active site. Surprisingly, there is no evidence of oligosaccharide binding in the active site of the enzyme. The closest bound oligosaccharide resides almost 18 Å from the active site. Mutations to conserved residues in binding sites I and VI had a debilitating effect on the activity of the enzyme.

PubMed: 26280198
DOI: 10.1021/acs.biochem.5b00228

実験手法

X-RAY DIFFRACTION (2.39 Å)