1OSM

OSMOPORIN (OMPK36) FROM KLEBSIELLA PNEUMONIAE

1OSM の概要

• エントリーDOI: 10.2210/pdb1osm/pdb
• 分子名称: OMPK36, DODECANE (2 entities in total)
• 機能のキーワード: outer membrane protein, non-specific porin, osmoporin, beta-barrel, transmembrane
• 由来する生物種: Klebsiella pneumoniae
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: Q48473
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 114424.45

構造登録者

Dutzler, R.,Schirmer, T. (登録日: 1999-01-08, 公開日: 1999-07-26, 最終更新日: 2024-05-22)

主引用文献

Dutzler, R.,Rummel, G.,Alberti, S.,Hernandez-Alles, S.,Phale, P.,Rosenbusch, J.,Benedi, V.,Schirmer, T.
Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae.
Structure Fold.Des., 7:425-434, 1999

PubMed Abstract: Porins are channel-forming membrane proteins that confer solute permeability to the outer membrane of Gram-negative bacteria. In Escherichia coli, major nonspecific porins are matrix porin (OmpF) and osmoporin (OmpC), which show high sequence homology. In response to high osmolarity of the medium, OmpC is expressed at the expense of OmpF porin. Here, we study osmoporin of the pathogenic Klebsiella pneumoniae (OmpK36), which shares 87% sequence identity with E. coliOmpC in an attempt to establish why osmoporin is best suited to function at high osmotic pressure.

PubMed: 10196126
DOI: 10.1016/S0969-2126(99)80055-0

実験手法

X-RAY DIFFRACTION (3.2 Å)