The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.
Structure and Function of TolC: The Bacterial Exit Duct for Proteins and Drugs
Abstract
▪ Abstract The bacterial TolC protein plays a common role in the expulsion of diverse molecules, which include protein toxins and antibacterial drugs, from the cell. TolC is a trimeric 12-stranded α/β barrel, comprising an α-helical trans-periplasmic tunnel embedded in the outer membrane by a contiguous β-barrel channel. This structure establishes a 140 Å long single pore fundamentally different to other membrane proteins and presents an exit duct to substrates, large and small, engaged at specific inner membrane translocases. TolC is open to the outside medium but is closed at its periplasmic entrance. When TolC is recruited by a substrate-laden translocase, the entrance is opened to allow substrate passage through a contiguous machinery spanning the entire cell envelope, from the cytosol to the external environment. Transition to the transient open state is achieved by an iris-like mechanism in which entrance α-helices undergo an untwisting realignment, thought to be stabilized by interaction with periplasmic helices of the translocase. TolC family proteins are ubiquitous among gram-negative bacteria, and the conserved entrance aperture presents a possible cheomotherapeutic target in multidrug-resistant pathogens.
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Citations
Cites
Multiple sequence alignment with hierarchical clustering
Corpet, F. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.22.10881 · Cited by 5,393
Type III Protein Secretion Systems in Bacterial Pathogens of Animals and Plants
Hueck, C. J. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.2.379-433.1998 · Cited by 2,394
Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore
Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., & Gouaux, J. E. (1996) · Science · doi:10.1126/science.274.5294.1859 · Cited by 2,377
Prevention of Drug Access to Bacterial Targets: Permeability Barriers and Active Efflux
Nikaido, H. (1994) · Science · doi:10.1126/science.8153625 · Cited by 1,540
Structure and function of bacterial outer membrane proteins: barrels in a nutshell
Koebnik, R., Locher, K. P., & Van Gelder, P. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01983.x · Cited by 1,202
Common Principles of Protein Translocation Across Membranes
Schatz, G., & Dobberstein, B. (1996) · Science · doi:10.1126/science.271.5255.1519 · Cited by 1,089
Koronakis, V., Sharff, A., Koronakis, E., Luisi, B., & Hughes, C. (2000) · Nature · doi:10.1038/35016007 · Cited by 1,086
Self-citationMultidrug efflux pumps of gram-negative bacteria
Nikaido, H. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.20.5853-5859.1996 · Cited by 1,082
Crystal structure of bacterial multidrug efflux transporter AcrB
Murakami, S., Nakashima, R., Yamashita, E., & Yamaguchi, A. (2002) · Nature · doi:10.1038/nature01050 · Cited by 986
Molecular Properties of Bacterial Multidrug Transporters
Putman, M., van Veen, H. W., & Konings, W. N. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.4.672-693.2000 · Cited by 795
Cited by
Clinically Relevant Chromosomally Encoded Multidrug Resistance Efflux Pumps in Bacteria
Piddock, L. J. V. (2006) · Clinical Microbiology Reviews · doi:10.1128/cmr.19.2.382-402.2006 · Cited by 1,231
Secretion systems in Gram-negative bacteria: Structural and mechanistic insights
Costa, T. R. D., Felisberto-Rodrigues, C., Meir, A., Prevost, M. S., Redzej, A., Trokter, M., & Waksman, G. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3456 · Cited by 1,132
Biosynthesis and Assembly of Capsular Polysaccharides in Escherichia coli
Whitfield, C. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142545 · Cited by 990
RTX proteins: a highly diverse family secreted by a common mechanism
Linhartová, I., Bumba, L., Mašín, J., Basler, M., Osička, R., Kamanová, J., Procházková, K., Adkins, I., Hejnová-Holubová, J., Sadílková, L., et al. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00231.x · Cited by 530
Hews, C. L., Cho, T., Rowley, G., & Raivio, T. L. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00313 · Cited by 168
Metadata
- Authors
- Koronakis, V., Eswaran, J., & Hughes, C.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2004-06
- Volume
- 73
- Issue
- 1
- Pages
- 467-489
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2167556437
- Cited by
- 357
- References
- 75
- FWCI
- 1.17
- Type
- journal article
- Language
- en
- Open access
- closed
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- Koronakis, V., Eswaran, J., & Hughes, C. (2004). Structure and Function of TolC: The Bacterial Exit Duct for Proteins and Drugs. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.73.011303.074104
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