Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily - PubMed (original) (raw)

. 2007 Aug 17;317(5840):957-61.

doi: 10.1126/science.1143860.

Affiliations

• PMID: 17702945
• DOI: 10.1126/science.1143860

Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily

Bernard Clantin et al. Science. 2007.

Abstract

In Gram-negative bacteria and eukaryotic organelles, beta-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 A crystal structure of FhaC. The transporter comprises a 16-stranded beta barrel that is occluded by an N-terminal alpha 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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Comment in

• Biochemistry. Getting into and through the outer membrane.
  Tommassen J. Tommassen J. Science. 2007 Aug 17;317(5840):903-4. doi: 10.1126/science.1146518. Science. 2007. PMID: 17702930 No abstract available.

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