1JW5

Structure of Maltose Bound to Open-form Maltodextrin-binding Protein in P1 Crystal

1JW5 の概要

• エントリーDOI: 10.2210/pdb1jw5/pdb
• 関連するPDBエントリー: 1ANF 1EZ9 1JW4 1OMP
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: maltodextrin-binding protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: sugar binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41095.45

構造登録者

Duan, X.,Quiocho, F.A. (登録日: 2001-09-02, 公開日: 2002-01-30, 最終更新日: 2024-02-07)

主引用文献

Duan, X.,Quiocho, F.A.
Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands.
Biochemistry, 41:706-712, 2002

PubMed Abstract: The receptor, a maltose/maltooligosaccharide-binding protein, has been found to be an excellent system for the study of molecular recognition because its polar and nonpolar binding functions are segregated into two globular domains. The X-ray structures of the "closed" and "open" forms of the protein complexed with maltose and maltotetraitol have been determined. These sugars have approximately 3 times more accessible polar surface (from OH groups) than nonpolar surface (from small clusters of sugar ring CH bonds). In the closed structures, the oligosaccharides are buried in the groove between the two domains of the protein and bound by extensive hydrogen bonding interactions of the OH groups with the polar residues confined mostly in one domain and by nonpolar interactions of the CH clusters with four aromatic residues lodged in the other domain. Substantial contacts between the sugar hydroxyls and aromatic residues are also formed. In the open structures, the oligosaccharides are bound almost exclusively in the domain rich in aromatic residues. This finding, along with the analysis of buried surface area due to complex formations in the open and closed structures, supports a major role for nonpolar interactions in initial ligand binding even when the ligands have significantly greater potential for highly specific polar interactions.

PubMed: 11790091
DOI: 10.1021/bi015784n

実験手法

X-RAY DIFFRACTION (2 Å)