4qky: Difference between revisions
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''' | ==Crystal Structure Analysis of the Membrane Transporter FhaC== | ||
<StructureSection load='4qky' size='340' side='right' caption='[[4qky]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4qky]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2qdz 2qdz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QKY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QKY FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qdz|2qdz]], [[4ql0|4ql0]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qky OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qky RCSB], [http://www.ebi.ac.uk/pdbsum/4qky PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:17702945</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Clantin, B.]] | |||
[[Category: Delattre, A S.]] | |||
[[Category: Dewitte, F.]] | |||
[[Category: Gruss, F.]] | |||
[[Category: Hiller, S.]] | |||
[[Category: Jacob-Dubuisson, F.]] | |||
[[Category: Maier, T.]] | |||
[[Category: Villeret, V.]] | |||
[[Category: Beta barrel]] | |||
[[Category: Outer membrane]] | |||
[[Category: Potra domain]] | |||
[[Category: Protein transport]] | |||
Revision as of 11:24, 22 October 2014
Crystal Structure Analysis of the Membrane Transporter FhaC
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