1MAL

STRUCTURAL BASIS FOR SUGAR TRANSLOCATION THROUGH MALTOPORIN CHANNELS AT 3.1 ANGSTROMS RESOLUTION

1MAL の概要

• エントリーDOI: 10.2210/pdb1mal/pdb
• 分子名称: MALTOPORIN (1 entity in total)
• 機能のキーワード: outer membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P02943
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 142277.36

構造登録者

Schirmer, T. (登録日: 1994-11-24, 公開日: 1995-12-31, 最終更新日: 2024-11-20)

主引用文献

Schirmer, T.,Keller, T.A.,Wang, Y.F.,Rosenbusch, J.P.
Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution.
Science, 267:512-514, 1995

PubMed Abstract: Trimeric maltoporin (LamB protein) facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The crystal structure of maltoporin from Escherichia coli, determined to a resolution of 3.1 angstroms, reveals an 18-stranded, antiparallel beta-barrel that forms the framework of the channel. Three inwardly folded loops contribute to a constriction about halfway through the channel. Six contingent aromatic residues line the channel and form a path from the vestibule to the periplasmic outlet. Soaking of a crystal with maltotriose revealed binding of the sugar to this hydrophobic track across the constriction, which suggests that maltose and linear oligosaccharides may be translocated across the membrane by guided diffusion along this path.

PubMed: 7824948

実験手法

X-RAY DIFFRACTION (3.1 Å)