6b12: Difference between revisions
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<StructureSection load='6b12' size='340' side='right' caption='[[6b12]], [[Resolution|resolution]] 1.71Å' scene=''> | <StructureSection load='6b12' size='340' side='right' caption='[[6b12]], [[Resolution|resolution]] 1.71Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6b12]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B12 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6b12]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Psef5 Psef5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B12 FirstGlance]. <br> | ||
</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> | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PFL_6209 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=220664 PSEF5]), PFL_6210 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=220664 PSEF5])</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=6b12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b12 OCA], [http://pdbe.org/6b12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b12 RCSB], [http://www.ebi.ac.uk/pdbsum/6b12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b12 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=6b12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b12 OCA], [http://pdbe.org/6b12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b12 RCSB], [http://www.ebi.ac.uk/pdbsum/6b12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b12 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The bacterial type VI secretion system (T6SS) mediates antagonistic cell-cell interactions between competing Gram-negative bacteria. In plant-beneficial bacteria, this pathway has been shown to suppress the growth of bacterial pathogens; however, the identification and mode of action of T6SS effector proteins that mediate this protective effect remain poorly defined. Here, we identify two previously uncharacterized effectors required for interbacterial antagonism by the plant commensal bacterium Pseudomonas protegens. Consistent with the established effectorimmunity paradigm for antibacterial T6SS substrates, the toxic activities of these effectors are neutralized by adjacently encoded cognate immunity determinants. While one of these effectors, RhsA, belongs to family of DNase enzymes, the activity of the other was not apparent from its sequence. To determine the mechanism of toxicity of this latter effector, we determined its 1.3A crystal structure in complex with its immunity protein and found that it resembles NAD(P)(+) degrading enzymes. In line with this structural similarity, biochemical characterization of this effector, termed Tne2 (<span style="text-decoration: underline;">t</span>ype VI secretion <span style="text-decoration: underline;">N</span>ADase <span style="text-decoration: underline;">e</span>ffector family 2), demonstrates that it possesses potent NAD(P)(+) hydrolase activity. Tne2 is the founding member of a widespread family of interbacterial NADases predicted to transit not only the Gramnegative T6SS but also the Gram-positive type VII secretion system, a pathway recently implicated in interbacterial competition among Firmicutes. Together, this work identifies new T6SS effectors employed by a plant commensal bacterium to antagonize its competitors and broadly implicates NAD(P)(+) hydrolyzing enzymes as substrates of interbacterial conflict pathways found in diverse bacterial phyla. | |||
Diverse NADase effector families mediate interbacterial antagonism via the type VI secretion system.,Tang JY, Bullen NP, Ahmad S, Whitney JC J Biol Chem. 2017 Dec 13. pii: RA117.000178. doi: 10.1074/jbc.RA117.000178. PMID:29237732<ref>PMID:29237732</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6b12" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Psef5]] | |||
[[Category: Tang, J Y]] | [[Category: Tang, J Y]] | ||
[[Category: Whitney, J C]] | [[Category: Whitney, J C]] | ||
Revision as of 11:59, 27 December 2017
Structure of Tne2 in complex with Tni2Structure of Tne2 in complex with Tni2
Structural highlights
Publication Abstract from PubMedThe bacterial type VI secretion system (T6SS) mediates antagonistic cell-cell interactions between competing Gram-negative bacteria. In plant-beneficial bacteria, this pathway has been shown to suppress the growth of bacterial pathogens; however, the identification and mode of action of T6SS effector proteins that mediate this protective effect remain poorly defined. Here, we identify two previously uncharacterized effectors required for interbacterial antagonism by the plant commensal bacterium Pseudomonas protegens. Consistent with the established effectorimmunity paradigm for antibacterial T6SS substrates, the toxic activities of these effectors are neutralized by adjacently encoded cognate immunity determinants. While one of these effectors, RhsA, belongs to family of DNase enzymes, the activity of the other was not apparent from its sequence. To determine the mechanism of toxicity of this latter effector, we determined its 1.3A crystal structure in complex with its immunity protein and found that it resembles NAD(P)(+) degrading enzymes. In line with this structural similarity, biochemical characterization of this effector, termed Tne2 (<span style="text-decoration: underline;">t</span>ype VI secretion <span style="text-decoration: underline;">N</span>ADase <span style="text-decoration: underline;">e</span>ffector family 2), demonstrates that it possesses potent NAD(P)(+) hydrolase activity. Tne2 is the founding member of a widespread family of interbacterial NADases predicted to transit not only the Gramnegative T6SS but also the Gram-positive type VII secretion system, a pathway recently implicated in interbacterial competition among Firmicutes. Together, this work identifies new T6SS effectors employed by a plant commensal bacterium to antagonize its competitors and broadly implicates NAD(P)(+) hydrolyzing enzymes as substrates of interbacterial conflict pathways found in diverse bacterial phyla. Diverse NADase effector families mediate interbacterial antagonism via the type VI secretion system.,Tang JY, Bullen NP, Ahmad S, Whitney JC J Biol Chem. 2017 Dec 13. pii: RA117.000178. doi: 10.1074/jbc.RA117.000178. PMID:29237732[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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