5j4a: Difference between revisions

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<StructureSection load='5j4a' size='340' side='right'caption='[[5j4a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5j4a' size='340' side='right'caption='[[5j4a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5j4a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J4A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5J4A FirstGlance]. <br>
<table><tr><td colspan='2'>[[5j4a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J4A FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j5v|5j5v]], [[5j43|5j43]]</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]] 2.004&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cdiA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 "Bacillus pseudomallei" Whitmore 1913]), cdiI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 "Bacillus pseudomallei" Whitmore 1913])</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=5j4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j4a OCA], [https://pdbe.org/5j4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j4a RCSB], [https://www.ebi.ac.uk/pdbsum/5j4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j4a ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5j4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j4a OCA], [http://pdbe.org/5j4a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j4a RCSB], [http://www.ebi.ac.uk/pdbsum/5j4a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j4a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CDIA9_BURPE CDIA9_BURPE]] Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. The C-terminal 160 residues (CT domain) acts as a general tRNA nuclease, and inhibits growth in E.coli. Cleaves specifically within the T-loop of E.coli tRNA2(Arg). Toxic activity is neutralized by coexpression of the cognate immunity protein CdiI in E.coli, but not by non-cognate immunity proteins from other strains of B.pseudomallei.<ref>PMID:22435733</ref> 
[https://www.uniprot.org/uniprot/CDIA9_BURPE CDIA9_BURPE] Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. The C-terminal 160 residues (CT domain) acts as a general tRNA nuclease, and inhibits growth in E.coli. Cleaves specifically within the T-loop of E.coli tRNA2(Arg). Toxic activity is neutralized by coexpression of the cognate immunity protein CdiI in E.coli, but not by non-cognate immunity proteins from other strains of B.pseudomallei.<ref>PMID:22435733</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Contact-dependent growth inhibition (CDI) is a wide-spread mechanism of inter-bacterial competition. CDI+ bacteria deploy large CdiA effector proteins, which carry variable C-terminal toxin domains (CdiA-CT). CDI+ cells also produce CdiI immunity proteins that specifically neutralize cognate CdiA-CT toxins to prevent auto-inhibition. Here, we present the crystal structure of the CdiA-CT/CdiIE479 toxin/immunity protein complex from Burkholderia pseudomallei isolate E479. The CdiA-CTE479 tRNase domain contains a core alpha/beta-fold that is characteristic of PD-(D/E)XK superfamily nucleases. Unexpectedly, the closest structural homolog of CdiA-CTE479 is another CDI toxin domain from B. pseudomallei 1026b. Though unrelated in sequence, the two B. pseudomallei nuclease domains share similar folds and active-site architectures. By contrast, the CdiIE479 and CdiI1026b immunity proteins share no significant sequence or structural homology. CdiA-CTE479 and CdiA-CT1026b are both tRNases, however the cleavage positions are different for each nuclease. We used a molecular docking approach to model each toxin bound to tRNA substrate. The resulting models fit into electron density envelopes generated by small-angle X-ray scattering analysis of stable complexes of tRNA bound to catalytically inactive toxin domains. CdiA-CTE479 is the third CDI toxin with structural homology to the PD-(D/E)XK superfamily. PD-(D/E)XK nucleases are characterized by highly variable sequences and active-site plasticity. CDI systems exploit this structural flexibility to generate toxin diversity. These findings raise the possibility that many other uncharacterized CDI toxins may also belong to the PD-(D/E)XK superfamily.
 
Functional Diversity of Cytotoxic tRNase/immunity Protein Complexes from Burkholderia pseudomallei.,Johnson PM, Gucinski GC, Garza-Sanchez F, Wong T, Hung LW, Hayes CS, Goulding CW J Biol Chem. 2016 Jul 20. pii: jbc.M116.736074. PMID:27445337<ref>PMID:27445337</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5j4a" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus pseudomallei whitmore 1913]]
[[Category: Burkholderia pseudomallei]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Goulding, C W]]
[[Category: Goulding CW]]
[[Category: Johnson, P M]]
[[Category: Johnson PM]]
[[Category: Complex]]
[[Category: Endonuclease]]
[[Category: Immunity protein]]
[[Category: Toxin]]