1OSM

OSMOPORIN (OMPK36) FROM KLEBSIELLA PNEUMONIAE

Summary for 1OSM

• Entry DOI: 10.2210/pdb1osm/pdb
• Descriptor: OMPK36, DODECANE (2 entities in total)
• Functional Keywords: outer membrane protein, non-specific porin, osmoporin, beta-barrel, transmembrane
• Biological source: Klebsiella pneumoniae
• Cellular location: Cell outer membrane; Multi-pass membrane protein: Q48473
• Total number of polymer chains: 3
• Total formula weight: 114424.45

Authors

Dutzler, R.,Schirmer, T. (deposition date: 1999-01-08, release date: 1999-07-26, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.2 Å)