The structure of porin from Rhodobacter capsulatus at 1.8 A resolution.
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.
Weiss
M S
MS
Institut für Organische Chemie und Biochemie der Universität, Freiburg, Germany.
Kreusch
A
A
Schiltz
E
E
Nestel
U
U
Welte
W
W
Weckesser
J
J
Schulz
G E
GE
D000596:Amino Acids / Q000032:analysis; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D006860:Hydrogen Bonding; D007473:Ion Channels / Q000737:chemistry; D008958:Models, Molecular; D018272:Porins; D011487:Protein Conformation; D016354:Rhodobacter capsulatus / Q000032:analysis*; D013237:Stereoisomerism; D014961:X-Ray Diffraction
D000596:Amino Acids; D001425:Bacterial Outer Membrane Proteins; D007473:Ion Channels; D018272:Porins