The three-dimensional structure of porin from Rhodobacter capsulatus at 3 A resolution.

M S Weiss, T Wacker, J Weckesser, W Welte, G E Schulz
Author Information
  1. M S Weiss: Institut für Organische Chemie und Biochemie, Freiburg, FRG.

Abstract

The crystal structure of porin from Rhodobacter capsulatus strain 37b4 has been solved at 3.0 A (1 A = 0.1 nm) resolution by multiple isomorphous replacement and solvent-flattening. The three pores of the trimer are well defined in the electron density map. Each pore consists of a 16-stranded beta-barrel which traverses the membrane as a tube. Near its center the tube is narrowed by chain segments protruding from the inner wall of the barrel that form an eye-let with an irregular cross-section of about 6 A by 10 A. The eye-let has an axial length of about 10 A; it defines the exclusion limit for diffusing particles.

MeSH Term

Bacterial Outer Membrane Proteins
Membrane Proteins
Models, Molecular
Porins
Protein Conformation
Rhodospirillaceae
X-Ray Diffraction

Chemicals

Bacterial Outer Membrane Proteins
Membrane Proteins
Porins

Word Cloud

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