2J1N

osmoporin OmpC

Summary for 2J1N

• Entry DOI: 10.2210/pdb2j1n/pdb
• Descriptor: OUTER MEMBRANE PROTEIN C, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: transport protein, beta-barrel, ion transport, osmoporin
• Biological source: ESCHERICHIA COLI
• Cellular location: Cell outer membrane; Multi-pass membrane protein: P06996
• Total number of polymer chains: 3
• Total formula weight: 117026.23

Authors

Basle, A.,Storici, P.,Rummel, G.,Rosenbusch, J.P.,Schirmer, T. (deposition date: 2006-08-15, release date: 2006-09-06, Last modification date: 2023-12-13)

Primary citation

Basle, A.,Rummel, G.,Storici, P.,Rosenbusch, J.P.,Schirmer, T.
Crystal Structure of Osmoporin Ompc from E. Coli at 2.0 A.
J.Mol.Biol., 362:933-, 2006

PubMed Abstract: Porins form transmembrane pores in the outer membrane of Gram-negative bacteria with matrix porin OmpF and osmoporin OmpC from Escherichia coli being differentially expressed depending on environmental conditions. The three-dimensional structure of OmpC has been determined to 2.0 A resolution by X-ray crystallography. As expected from the high sequence similarity, OmpC adopts the OmpF-like 16-stranded hollow beta-barrel fold with three beta-barrels associated to form a tight trimer. Unlike in OmpF, the extracellular loops form a continuous wall at the perimeter of the vestibule common to the three pores, due to a 14-residues insertion in loop L4. The pore constriction and the periplasmic outlet are very similar to OmpF with 74% of the pore lining residues being conserved. Overall, only few ionizable residues are exchanged at the pore lining. The OmpC structure suggests that not pore size, but electrostatic pore potential and particular atomic details of the pore linings are the critical parameters that physiologically distinguish OmpC from OmpF.

PubMed: 16949612
DOI: 10.1016/J.JMB.2006.08.002

Experimental method

X-RAY DIFFRACTION (2 Å)