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 | 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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:38:30 2008'' | ||