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==Crystal structure of Francisella tularensis REP34 (Rapid Encystment Phenotype Protein 34 KDa)==
==Crystal structure of Francisella tularensis REP34 (Rapid Encystment Phenotype Protein 34 KDa)==
<StructureSection load='4oko' size='340' side='right' caption='[[4oko]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='4oko' size='340' side='right'caption='[[4oko]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4oko]] is a 4 chain structure. 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><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><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.053&#8491;</td></tr>
<tr><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://www.rcsb.org/pdb/explore.do?structureId=4oko RCSB], [http://www.ebi.ac.uk/pdbsum/4oko PDBsum]</span></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>
<table>
<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>
<div style="background-color:#fffaf0;">
</table>
== Publication Abstract from PubMed ==
== Function ==
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.
[https://www.uniprot.org/uniprot/A0Q494_FRATN A0Q494_FRATN]
 
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<ref>PMID:25231992</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Corzett, M H.]]
[[Category: Francisella tularensis subsp. novicida U112]]
[[Category: Feld, G K.]]
[[Category: Large Structures]]
[[Category: Frank, M.]]
[[Category: Corzett MH]]
[[Category: Hunter, M S.]]
[[Category: Feld GK]]
[[Category: Rasley, A.]]
[[Category: Frank M]]
[[Category: Segelke, B W.]]
[[Category: Hunter MS]]
[[Category: Carboxypeptidase]]
[[Category: Rasley A]]
[[Category: Hydrolase]]
[[Category: Segelke BW]]
[[Category: Secreted]]
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