2qdz: Difference between revisions

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New page: left|200px<br /><applet load="2qdz" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qdz, resolution 3.15Å" /> '''Structure of the mem...
 
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==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
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[[Category: protein transport]]
[[Category: protein transport]]


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