Molecular Architecture and Electrostatic Properties of a Bacterial Porin

• Published in: Science (American Association for the Advancement of Science) Vol. 254; no. 5038; pp. 1627 - 1630
• Main Authors: Weiss, M. S., Abele, U., Weckesser, J., Welte, W., Schiltz, E., Schulz, G. E.
• Format: Journal Article
• Language: English
• Published: United States American Society for the Advancement of Science 13-12-1991; American Association for the Advancement of Science; The American Association for the Advancement of Science
• Subjects: Atoms; Bacteria; Bacterial Outer Membrane Proteins - chemistry; Biochemistry; Calcium; Calcium - metabolism; Calcium-Binding Proteins - metabolism; Computer Graphics; Crystallography; Electrical potential; Electrostatics; Ion Channels - chemistry; Ions; Macromolecular Substances; Membrane proteins; Models, Molecular; Molecular Structure; Molecules; Porins; Protein Conformation; Proteins; Rhodobacter capsulatus; Rhodobacter capsulatus - chemistry; Solutes; Trimers; X-ray crystallography; X-Ray Diffraction
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.1721242

The integral membrane protein porin from Rhodobacter capsulatus consists of three tightly associated 16-stranded β 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 Ca$^{2+}$ sites.