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==Crystal structure of CdiA-CT/CdiI complex from Y. kristensenii 33638==
==Crystal structure of CdiA-CT/CdiI complex from Y. kristensenii 33638==
<StructureSection load='5e3e' size='340' side='right' caption='[[5e3e]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='5e3e' size='340' side='right'caption='[[5e3e]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5e3e]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E3E FirstGlance]. <br>
<table><tr><td colspan='2'>[[5e3e]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_kristensenii_ATCC_33638 Yersinia kristensenii ATCC 33638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E3E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.7&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5e3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e3e OCA], [http://pdbe.org/5e3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e3e RCSB], [http://www.ebi.ac.uk/pdbsum/5e3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e3e 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=5e3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e3e OCA], [https://pdbe.org/5e3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e3e RCSB], [https://www.ebi.ac.uk/pdbsum/5e3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e3e ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Contact-dependent growth inhibition (CDI) is an important mechanism of inter-bacterial competition found in many Gram-negative pathogens. CDI+ cells express cell-surface CdiA proteins that bind neighboring bacteria and deliver C-terminal toxin domains (CdiA-CT) to inhibit target-cell growth. CDI+ bacteria also produce CdiI immunity proteins, which specifically neutralize cognate CdiA-CT toxins to prevent self-inhibition. Here, we present the crystal structure of the CdiA-CT/CdiIYkris complex from Yersinia kristensenii ATCC 33638. CdiA-CTYkris adopts the same fold as angiogenin and other RNase A paralogs, but the toxin does not share sequence similarity with these nucleases and lacks the characteristic disulfide bonds of the superfamily. Consistent with the structural homology, CdiA-CTYkris has potent RNase activity in vitro and in vivo. Structure-guided mutagenesis reveals that His175, Arg186, Thr276 and Tyr278 contribute to CdiA-CTYkris activity, suggesting that these residues participate in substrate binding and/or catalysis. CdiIYkris binds directly over the putative active site and likely neutralizes toxicity by blocking access to RNA substrates. Significantly, CdiA-CTYkris is the first non-vertebrate protein found to possess the RNase A superfamily fold, and homologs of this toxin are associated with secretion systems in many Gram-negative and Gram-positive bacteria. These observations suggest that RNase A-like toxins are commonly deployed in inter-bacterial competition.
The CDI toxin of Yersinia kristensenii is a novel bacterial member of the RNase A superfamily.,Batot G, Michalska K, Ekberg G, Irimpan EM, Joachimiak G, Jedrzejczak R, Babnigg G, Hayes CS, Joachimiak A, Goulding CW Nucleic Acids Res. 2017 May 19;45(9):5013-5025. doi: 10.1093/nar/gkx230. PMID:28398546<ref>PMID:28398546</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5e3e" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Goulding, C W]]
[[Category: Large Structures]]
[[Category: Jedrzejczak, R]]
[[Category: Yersinia kristensenii ATCC 33638]]
[[Category: Joachimiak, A]]
[[Category: Goulding CW]]
[[Category: Joachimiak, G]]
[[Category: Jedrzejczak R]]
[[Category: Structural genomic]]
[[Category: Joachimiak A]]
[[Category: Michalska, K]]
[[Category: Joachimiak G]]
[[Category: UC4CDI, Structure-Function Analysis of Polymorphic CDI Toxin-Immunity Protein Complexes]]
[[Category: Michalska K]]
[[Category: Immunity protein]]
[[Category: Mcsg]]
[[Category: Nuclease]]
[[Category: Psi-biology]]
[[Category: Structure-function analysis of polymorphic cdi toxin-immunity protein complex]]
[[Category: Toxin]]
[[Category: Uc4cdi]]
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