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3POR

PORIN CONFORMATION IN THE ABSENCE OF CALCIUM; REFINED STRUCTURE AT 2.5 ANGSTROMS RESOLUTION

Summary for 3POR
Entry DOI10.2210/pdb3por/pdb
DescriptorPORIN, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
Functional Keywordsintegral membrane protein porin
Biological sourceRhodobacter capsulatus
Cellular locationCell outer membrane; Multi-pass membrane protein: P31243
Total number of polymer chains1
Total formula weight31984.00
Authors
Weiss, M.S.,Schulz, G.E. (deposition date: 1992-11-09, release date: 1993-07-15, Last modification date: 2024-02-21)
Primary citationWeiss, M.S.,Schulz, G.E.
Porin conformation in the absence of calcium. Refined structure at 2.5 A resolution.
J.Mol.Biol., 231:817-824, 1993
Cited by
PubMed Abstract: 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.
PubMed: 7685826
DOI: 10.1006/jmbi.1993.1328
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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