2J1N

osmoporin OmpC

2J1N の概要

• エントリーDOI: 10.2210/pdb2j1n/pdb
• 分子名称: OUTER MEMBRANE PROTEIN C, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: transport protein, beta-barrel, ion transport, osmoporin
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P06996
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 117026.23

構造登録者

Basle, A.,Storici, P.,Rummel, G.,Rosenbusch, J.P.,Schirmer, T. (登録日: 2006-08-15, 公開日: 2006-09-06, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)