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| | <StructureSection load='4oko' size='340' side='right'caption='[[4oko]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='4oko' size='340' side='right'caption='[[4oko]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4oko]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Fratn Fratn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OKO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OKO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4oko]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._novicida_U112 Francisella tularensis subsp. novicida U112]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OKO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTN_0149 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=401614 FRATN])</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=4oko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oko OCA], [https://pdbe.org/4oko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oko RCSB], [https://www.ebi.ac.uk/pdbsum/4oko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oko ProSAT]</span></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=4oko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oko OCA], [http://pdbe.org/4oko PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oko RCSB], [http://www.ebi.ac.uk/pdbsum/4oko PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oko ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0Q494_FRATN A0Q494_FRATN] |
| | <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: Fratn]] | + | [[Category: Francisella tularensis subsp. novicida U112]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Corzett, M H]] | + | [[Category: Corzett MH]] |
| - | [[Category: Feld, G K]] | + | [[Category: Feld GK]] |
| - | [[Category: Frank, M]] | + | [[Category: Frank M]] |
| - | [[Category: Hunter, M S]] | + | [[Category: Hunter MS]] |
| - | [[Category: Rasley, A]] | + | [[Category: Rasley A]] |
| - | [[Category: Segelke, B W]] | + | [[Category: Segelke BW]] |
| - | [[Category: Carboxypeptidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Secreted]]
| + | |
| Structural highlights
Function
A0Q494_FRATN
Publication Abstract from PubMed
Francisella tularensis is the etiological agent of tularemia, or rabbit fever. While F. tularensis is a recognized biothreat agent with broad and expanding geographical range, its mechanism of infection and environmental persistence remain poorly understood. Previously, we identified seven F. tularensis proteins that induce a rapid encystment phenotype (REP) in the free-living amoeba, Acanthamoeba castellanii. Encystment is essential to the pathogen's long-term intracellular survival in amoeba. Here, we characterize the cellular and molecular function of REP34, a REP protein of mass 34 kDa. A REP34 knockout strain of F. tularensis has a reduced ability to both induce encystment in A. castellanii and invade human macrophages. We determined the crystal structure of REP34 to 2.05-A resolution and demonstrate robust carboxypeptidase B-like activity for the enzyme. REP34 is a zinc-containing monomeric protein with close structural homology to the metallocarboxypeptidase family of peptidases. REP34 possesses a novel topology and substrate binding pocket that deviates from the canonical funnelin structure of carboxypeptidases, putatively resulting in a catalytic role for a conserved tyrosine and distinct S1' recognition site. Taken together, these results identify REP34 as an active carboxypeptidase, implicate the enzyme as a potential key F. tularensis effector protein, and may help elucidate a mechanistic understanding of F. tularensis infection of phagocytic cells.
Structure and function of REP34 implicates carboxypeptidase activity in Francisella tularensis host-cell invasion.,Feld GK, El-Etr S, Corzett MH, Hunter MS, Belhocine K, Monack DM, Frank M, Segelke BW, Rasley A J Biol Chem. 2014 Sep 17. pii: jbc.M114.599381. PMID:25231992[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feld GK, El-Etr S, Corzett MH, Hunter MS, Belhocine K, Monack DM, Frank M, Segelke BW, Rasley A. Structure and function of REP34 implicates carboxypeptidase activity in Francisella tularensis host-cell invasion. J Biol Chem. 2014 Sep 17. pii: jbc.M114.599381. PMID:25231992 doi:http://dx.doi.org/10.1074/jbc.M114.599381
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