Structural highlights
Function
[PORI_RHOCA] Forms channels that allow the passive diffusion of small hydrophilic solutes up to an exclusion limit of about 0.6 kDa.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of porin from Rhodobacter capsulatus in the absence of divalent calcium ions has been refined to convergence at a resolution of 2.5 A using the simulated annealing refinement method. The final model consists of all 301 amino acid residues, 77 solvent molecules, one tris(hydroxymethyl)-aminomethane molecule and one unknown ligand modeled as n-octyltetraoxyethylene. A superposition with the previously described model containing three calcium ions showed structural changes at the segment 108-116 of the inner loop beta 5-beta 6, and at loops beta 8-beta 9 and beta 11-beta 12 at the extracellular side of the porin molecule. Evidence is presented that the conformational changes depend on the presence or absence of calcium ions. A possible influence on porin function is discussed.
Porin conformation in the absence of calcium. Refined structure at 2.5 A resolution.,Weiss MS, Schulz GE J Mol Biol. 1993 Jun 5;231(3):817-24. PMID:7685826[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Weiss MS, Schulz GE. Porin conformation in the absence of calcium. Refined structure at 2.5 A resolution. J Mol Biol. 1993 Jun 5;231(3):817-24. PMID:7685826 doi:http://dx.doi.org/10.1006/jmbi.1993.1328
