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PMID: 2165921 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 267 ·No. 2 ·1990-07-16 ·Pages 268-72

Weiss MS, Wacker T, Weckesser J, Welte W, Schulz GE

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 Terms
Bacterial Outer Membrane Proteins/isolation & purification Membrane Proteins/isolation & purification Models, Molecular Porins Protein Conformation Rhodospirillaceae/analysis X-Ray Diffraction
Chemicals
Bacterial Outer Membrane Proteins Membrane Proteins Porins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Weiss M S
Institut für Organische Chemie und Biochemie, Freiburg, FRG.
Wacker T
Weckesser J
Welte W
Schulz G E
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1990-07-16
Pages
268-72
Language
English
Region
England
NLM ID
0155157
Subset
IM
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