The structure of porin from Paracoccus denitrificans at 3.1 A resolution

FEBS Lett. 1997 Mar 10;404(2-3):208-10. doi: 10.1016/s0014-5793(97)00131-2.

Abstract

The crystal structure of a non-specific porin from Paracoccus denitrificans at 3.1 A resolution has been solved by molecular replacement using the porin from Rhodopseudomonas blastica as the search model. Paracoccus porin is very similar to other non-specific porins of known structure: a trimer of 16 stranded beta-barrels each with a central pore constricted by a long extracellular loop folding back against the barrel wall. The distinctive distribution of charged residues of this non-specific porin contributes to understanding the relation between structure and ion selectivity.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Models, Molecular
  • Paracoccus denitrificans*
  • Porins / chemistry*
  • Protein Structure, Secondary*
  • Rhodopseudomonas

Substances

  • Porins