4ql0: Difference between revisions

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'''Unreleased structure'''
==Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)==
<StructureSection load='4ql0' size='340' side='right' caption='[[4ql0]], [[Resolution|resolution]] 2.50&Aring;' 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.


The entry 4ql0 is ON HOLD  until Paper Publication
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>


Authors: Maier, T., Clantin, B., Gruss, F., Dewitte, F., Delattre, A.S., Jacob-Dubuisson, F., Hiller, S., Villeret, V.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)
== References ==
[[Category: Unreleased Structures]]
<references/>
__TOC__
</StructureSection>
[[Category: Clantin, B]]
[[Category: Clantin, B]]
[[Category: Maier, T]]
[[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: Delattre, A.S]]
[[Category: Beta-barrel]]
[[Category: Dewitte, F]]
[[Category: Outer membrane]]
[[Category: Gruss, F]]
[[Category: Potra domain]]
[[Category: Protein transport]]