The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Structure of the Membrane Protein FhaC: A Member of the Omp85-TpsB Transporter Superfamily
Abstract
In Gram-negative bacteria and eukaryotic organelles, β-barrel proteins of the outer membrane protein 85–two-partner secretion B (Omp85-TpsB) superfamily are essential components of protein transport machineries. The TpsB transporter FhaC mediates the secretion of Bordetella pertussis filamentous hemagglutinin (FHA). We report the 3.15 Å crystal structure of FhaC. The transporter comprises a 16-stranded β barrel that is occluded by an N-terminal α helix and an extracellular loop and a periplasmic module composed of two aligned polypeptide-transport–associated (POTRA) domains. Functional data reveal that FHA binds to the POTRA 1 domain via its N-terminal domain and likely translocates the adhesin-repeated motifs in an extended hairpin conformation, with folding occurring at the cell surface. General features of the mechanism obtained here are likely to apply throughout the superfamily.
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Self-citation
Metadata
- Authors
- Clantin, B., Delattre, A.-S., Rucktooa, P., Saint, N., Méli, A. C., Locht, C., Jacob-Dubuisson, F., & Villeret, V.
- Venue
- Science
- Published
- 2007-08-17
- Volume
- 317
- Issue
- 5840
- Pages
- 957-961
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2059000517
- Cited by
- 255
- References
- 25
- FWCI
- 13.40
- Type
- journal article
- Language
- en
- Open access
- closed
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- Clantin, B., Delattre, A.-S., Rucktooa, P., Saint, N., Méli, A. C., Locht, C., Jacob-Dubuisson, F., & Villeret, V. (2007). Structure of the Membrane Protein FhaC: A Member of the Omp85-TpsB Transporter Superfamily. Science. https://doi.org/10.1126/science.1143860
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