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| | ==Crystal structure of the R450A mutant of the membrane protein FhaC== | | ==Crystal structure of the R450A mutant of the membrane protein FhaC== |
| - | <StructureSection load='3njt' size='340' side='right' caption='[[3njt]], [[Resolution|resolution]] 3.50Å' scene=''> | + | <StructureSection load='3njt' size='340' side='right'caption='[[3njt]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3njt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_tussis-convulsivae"_lehmann_and_neumann_1927 "bacterium tussis-convulsivae" lehmann and neumann 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NJT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3njt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NJT FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fhaC, BP1884 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=520 "Bacterium tussis-convulsivae" Lehmann and Neumann 1927])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</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=3njt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3njt OCA], [http://pdbe.org/3njt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3njt RCSB], [http://www.ebi.ac.uk/pdbsum/3njt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3njt ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3njt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3njt OCA], [https://pdbe.org/3njt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3njt RCSB], [https://www.ebi.ac.uk/pdbsum/3njt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3njt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium tussis-convulsivae lehmann and neumann 1927]] | + | [[Category: Bordetella pertussis]] |
| - | [[Category: Clantin, B]] | + | [[Category: Large Structures]] |
| - | [[Category: Delattre, A S]] | + | [[Category: Clantin B]] |
| - | [[Category: Jacob-Dubuisson, F]] | + | [[Category: Delattre AS]] |
| - | [[Category: Villeret, V]] | + | [[Category: Jacob-Dubuisson F]] |
| - | [[Category: Beta barrel]]
| + | [[Category: Villeret V]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Omp85/tpsb transporter family]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| Structural highlights
Function
FHAC_BORPE Member of a two partner secretion pathway (TPS) in which it mediates the secretion of filamentous hemagglutinin (FHA).[1]
Publication Abstract from PubMed
In Gram-negative bacteria, the two-partner secretion pathway mediates the secretion of TpsA proteins with various functions. TpsB transporters specifically recognize their TpsA partners in the periplasm and mediate their transport through a hydrophilic channel. The filamentous haemagglutinin adhesin (FHA)/FhaC pair represents a model two-partner secretion system, with the structure of the TpsB transporter FhaC providing the bases to decipher the mechanism of action of these proteins. FhaC is composed of a beta-barrel preceded by two periplasmic polypeptide-transport-associated (POTRA) domains in tandem. The barrel is occluded by an N-terminal helix and an extracellular loop, L6, folded back into the FhaC channel. In this article, we describe a functionally important motif of FhaC. The VRGY tetrad is highly conserved in the TpsB family and, in FhaC, it is located at the tip of L6 reaching the periplasm. Replacement by Ala of the invariant Arg dramatically affects the secretion efficiency, although the structure of FhaC and its channel properties remain unaffected. This substitution affects the secretion mechanism at a step beyond the initial TpsA-TpsB interaction. Replacement of the conserved Tyr affects the channel properties, but not the secretion activity, suggesting that this residue stabilizes the loop in the resting conformation of FhaC. Thus, the conserved motif at the tip of L6 represents an important piece of two-partner secretion machinery. This motif is conserved in a predicted loop between two beta-barrel strands in more distant relatives of FhaC involved in protein transport across or assembly into the outer membranes of bacteria and organelles, suggesting a conserved function in the molecular mechanism of transport.
Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily.,Delattre AS, Clantin B, Saint N, Locht C, Villeret V, Jacob-Dubuisson F FEBS J. 2010 Nov;277(22):4755-65. doi: 10.1111/j.1742-4658.2010.07881.x., Epub 2010 Oct 19. PMID:20955520[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hodak H, Clantin B, Willery E, Villeret V, Locht C, Jacob-Dubuisson F. Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate. Mol Microbiol. 2006 Jul;61(2):368-82. Epub 2006 Jun 12. PMID:16771844 doi:10.1111/j.1365-2958.2006.05242.x
- ↑ Delattre AS, Clantin B, Saint N, Locht C, Villeret V, Jacob-Dubuisson F. Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily. FEBS J. 2010 Nov;277(22):4755-65. doi: 10.1111/j.1742-4658.2010.07881.x., Epub 2010 Oct 19. PMID:20955520 doi:10.1111/j.1742-4658.2010.07881.x
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