4qky
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4qky]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis_Tohama_I Bordetella pertussis Tohama I]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QKY FirstGlance]. <br> | <table><tr><td colspan='2'>[[4qky]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis_Tohama_I Bordetella pertussis Tohama I]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QKY FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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]] 2.9Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4qky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qky OCA], [https://pdbe.org/4qky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qky RCSB], [https://www.ebi.ac.uk/pdbsum/4qky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qky 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=4qky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qky OCA], [https://pdbe.org/4qky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qky RCSB], [https://www.ebi.ac.uk/pdbsum/4qky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qky ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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> | [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;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4qky" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal Structure Analysis of the Membrane Transporter FhaC
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