1M5Y

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

1M5Y の概要

• エントリーDOI: 10.2210/pdb1m5y/pdb
• 分子名称: Survival protein surA (1 entity in total)
• 機能のキーワード: survival protein a, periplasmic molecular chaperone, membrane protein folding, gram negative bacteria, isomerase, cell cycle
• 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: 180527.70

構造登録者

Bitto, E.,McKay, D.B. (登録日: 2002-07-10, 公開日: 2002-11-08, 最終更新日: 2024-02-14)

主引用文献

Bitto, E.,McKay, D.B.
Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Folding of Outer Membrane Porins
Structure, 10:1489-1498, 2002

PubMed Abstract: The SurA protein facilitates correct folding of outer membrane proteins in gram-negative bacteria. The sequence of Escherichia coli SurA presents four segments, two of which are peptidyl-prolyl isomerases (PPIases); the crystal structure reveals an asymmetric dumbbell, in which the amino-terminal, carboxy-terminal, and first PPIase segments of the sequence form a core structural module, and the second PPIase segment is a satellite domain tethered approximately 30 A from this module. The core module, which is implicated in membrane protein folding, has a novel fold that includes an extended crevice. Crystal contacts show that peptides bind within the crevice, suggesting a model for chaperone activity whereby segments of polypeptide may be repetitively sequestered and released during the membrane protein-folding process.

PubMed: 12429090
DOI: 10.1016/S0969-2126(02)00877-8

実験手法

X-RAY DIFFRACTION (3 Å)