The structure of porin from Rhodobacter capsulatus at 1.8 A resolution.

M S Weiss, A Kreusch, E Schiltz, U Nestel, W Welte, J Weckesser, G E Schulz
Author Information
  1. M S Weiss: Institut für Organische Chemie und Biochemie der Universität, Freiburg, Germany.

Abstract

The structure of the porin from Rhodobacter capsulatus was determined at a resolution of 1.8 A. The analysis started from a closely related crystal structure that had been solved at a medium resolution of 3 A using multiple isomorphous replacement and solvent flattening. The new structure contains the complete sequence of 301 amino acid residues. Refinement of the model is under way; the present R-factor is 22% with good geometry. Except for the lengths of several loops, the resulting chain fold corresponds to the medium resolution model. The membrane channel is lined by a large number of ionogenic side chains with characteristic segregation of differently charged groups.

MeSH Term

Amino Acids
Bacterial Outer Membrane Proteins
Hydrogen Bonding
Ion Channels
Models, Molecular
Porins
Protein Conformation
Rhodobacter capsulatus
Stereoisomerism
X-Ray Diffraction

Chemicals

Amino Acids
Bacterial Outer Membrane Proteins
Ion Channels
Porins

Word Cloud

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