Molecular architecture and electrostatic properties of a bacterial porin.
The integral membrane protein porin from Rhodobacter capsulatus consists of three tightly associated 16-stranded beta barrels that give rise to three distinct diffusion channels for small solutes through the outer membrane. The x-ray structure of this porin has revealed details of its shape, the residue distributions within the pore and at the membrane-facing surface, and the location of calcium sites. The electrostatic potential has been calculated and related to function. Moreover, potential calculations were found to predict the Ca2+ sites.
Weiss
M S
MS
Institut für Organische Chemie und Biochemie, Freiburg, Federal Republic of Germany.
Abele
U
U
Weckesser
J
J
Welte
W
W
Schiltz
E
E
Schulz
G E
GE
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000378:metabolism; D003196:Computer Graphics; D003461:Crystallography; D007473:Ion Channels / Q000737:chemistry*; D007477:Ions; D046911:Macromolecular Substances; D008958:Models, Molecular; D015394:Molecular Structure; D018272:Porins; D011487:Protein Conformation; D016354:Rhodobacter capsulatus / Q000737:chemistry*; D014961:X-Ray Diffraction
D001425:Bacterial Outer Membrane Proteins; D002135:Calcium-Binding Proteins; D007473:Ion Channels; D007477:Ions; D046911:Macromolecular Substances; D018272:Porins; D002118:Calcium