2qdz
From Proteopedia
(New page: 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'' |
Revision as of 16:38, 21 February 2008
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Structure of the membrane protein fhac: a member of the omp85/tpsb transporter family
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.
About this Structure
2QDZ is a Single protein structure of sequence from Bordetella pertussis. Full crystallographic information is available from OCA.
Reference
Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily., Clantin B, Delattre AS, Rucktooa P, Saint N, Meli AC, Locht C, Jacob-Dubuisson F, Villeret V, Science. 2007 Aug 17;317(5840):957-61. PMID:17702945
Page seeded by OCA on Thu Feb 21 18:38:30 2008
