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4ql0

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==Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)==
==Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)==
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<StructureSection load='4ql0' size='340' side='right' caption='[[4ql0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='4ql0' size='340' side='right'caption='[[4ql0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[4ql0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis_Tohama_I Bordetella pertussis Tohama I]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QL0 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qky|4qky]], [[2qdz|2qdz]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ql0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ql0 OCA], [https://pdbe.org/4ql0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ql0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ql0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ql0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[https://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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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.
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Omp85 proteins mediate translocation of polypeptide substrates across and into cellular membranes. They share a common architecture comprising substrate-interacting POTRA domains, a C-terminal 16-stranded beta-barrel pore and two signature motifs located on the inner barrel wall and at the tip of the extended L6 loop. The observation of two distinct conformations of the L6 loop in the available Omp85 structures previously suggested a functional role of conformational changes in L6 in the Omp85 mechanism. Here we present a 2.5 A resolution structure of a variant of the Omp85 secretion protein FhaC, in which the two signature motifs interact tightly and form the conserved 'lid lock'. Reanalysis of previous structural data shows that L6 adopts the same, conserved resting state position in all available Omp85 structures. The FhaC variant structure further reveals a competitive mechanism for the regulation of substrate binding mediated by the linker to the N-terminal plug helix H1.
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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>
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Conserved Omp85 lid-lock structure and substrate recognition in FhaC.,Maier T, Clantin B, Gruss F, Dewitte F, Delattre AS, Jacob-Dubuisson F, Hiller S, Villeret V Nat Commun. 2015 Jun 10;6:7452. doi: 10.1038/ncomms8452. PMID:26058369<ref>PMID:26058369</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4ql0" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Clantin, B]]
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[[Category: Bordetella pertussis Tohama I]]
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[[Category: Delattre, A S]]
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[[Category: Large Structures]]
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[[Category: Dewitte, F]]
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[[Category: Clantin B]]
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[[Category: Gruss, F]]
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[[Category: Delattre AS]]
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[[Category: Hiller, S]]
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[[Category: Dewitte F]]
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[[Category: Jacob-Dubuisson, F]]
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[[Category: Gruss F]]
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[[Category: Maier, T]]
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[[Category: Hiller S]]
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[[Category: Villeret, V]]
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[[Category: Jacob-Dubuisson F]]
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[[Category: Beta-barrel]]
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[[Category: Maier T]]
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[[Category: Outer membrane]]
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[[Category: Villeret V]]
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[[Category: Potra domain]]
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[[Category: Protein transport]]
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Current revision

Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)

PDB ID 4ql0

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