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Molecular Architecture and Electrostatic Properties of a Bacterial Porin
Abstract
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.
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Citations
Cited by
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MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
White, S. H., & Wimley, W. C. (1999) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.28.1.319 · Cited by 1,764
Structure of the MscL Homolog from Mycobacterium tuberculosis : A Gated Mechanosensitive Ion Channel
Chang, G., Spencer, R. H., Lee, A. T., Barclay, M. T., & Rees, D. C. (1998) · Science · doi:10.1126/science.282.5397.2220 · Cited by 990
Structural Basis for Sugar Translocation Through Maltoporin Channels at 3.1 Å Resolution
Schirmer, T., Keller, T. A., Wang, Y.-F., & Rosenbusch, J. P. (1995) · Science · doi:10.1126/science.7824948 · Cited by 593
Transmembrane Signaling across the Ligand-Gated FhuA Receptor
Locher, K. P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J. P., & Moras, D. (1998) · Cell · doi:10.1016/s0092-8674(00)81700-6 · Cited by 540
Metadata
- Authors
- Weiss, M. S., Abele, U., Weckesser, J., Welte, W., Schiltz, E., & Schulz, G. E.
- Venue
- Science
- Published
- 1991-12-13
- Volume
- 254
- Issue
- 5038
- Pages
- 1627-1630
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2086881332
- Cited by
- 702
- References
- 0
- FWCI
- 24.61
- Type
- journal article
- Language
- en
- Open access
- closed
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- Weiss, M. S., Abele, U., Weckesser, J., Welte, W., Schiltz, E., & Schulz, G. E. (1991). Molecular Architecture and Electrostatic Properties of a Bacterial Porin. Science. https://doi.org/10.1126/science.1721242
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
