4ql0
From Proteopedia
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| - | ''' | + | ==Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)== |
| + | <StructureSection load='4ql0' size='340' side='right' caption='[[4ql0]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ql0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QL0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QL0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <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">[[4qky|4qky]], [[2qdz|2qdz]]</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=4ql0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ql0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ql0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ql0 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FHAC_BORPE FHAC_BORPE]] Member of a two partner secretion pathway (TPS) in which it mediates the secretion of filamentous hemagglutinin (FHA).<ref>PMID:16771844</ref> | ||
| + | <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: Clantin, B]] | ||
| - | [[Category: | + | [[Category: Delattre, A S]] |
| + | [[Category: Dewitte, F]] | ||
| + | [[Category: Gruss, F]] | ||
[[Category: Hiller, S]] | [[Category: Hiller, S]] | ||
[[Category: Jacob-Dubuisson, F]] | [[Category: Jacob-Dubuisson, F]] | ||
| + | [[Category: Maier, T]] | ||
[[Category: Villeret, V]] | [[Category: Villeret, V]] | ||
| - | [[Category: | + | [[Category: Beta-barrel]] |
| - | [[Category: | + | [[Category: Outer membrane]] |
| - | [[Category: | + | [[Category: Potra domain]] |
| + | [[Category: Protein transport]] | ||
Revision as of 15:12, 17 June 2015
Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)
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