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7ljn

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Current revision (14:59, 6 March 2024) (edit) (undo)
 
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<StructureSection load='7ljn' size='340' side='right'caption='[[7ljn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='7ljn' size='340' side='right'caption='[[7ljn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7ljn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/3i1b110 3i1b110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LJN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7ljn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_diazoefficiens Bradyrhizobium diazoefficiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LJN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blr0072 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1355477 3I1B110])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=7ljn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ljn OCA], [https://pdbe.org/7ljn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ljn RCSB], [https://www.ebi.ac.uk/pdbsum/7ljn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ljn 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=7ljn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ljn OCA], [https://pdbe.org/7ljn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ljn RCSB], [https://www.ebi.ac.uk/pdbsum/7ljn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ljn ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q89Y83_BRADU Q89Y83_BRADU]
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cGAS/DncV-like nucleotidyltransferase (CD-NTase) enzymes are signaling proteins that initiate antiviral immunity in animal cells and cyclic-oligonucleotide-based anti-phage signaling system (CBASS) phage defense in bacteria. Upon phage recognition, bacterial CD-NTases catalyze synthesis of cyclic-oligonucleotide signals, which activate downstream effectors and execute cell death. How CD-NTases control nucleotide selection to specifically induce defense remains poorly defined. Here, we combine structural and nucleotide-analog interference-mapping approaches to identify molecular rules controlling CD-NTase specificity. Structures of the cyclic trinucleotide synthase Enterobacter cloacae CdnD reveal coordinating nucleotide interactions and a possible role for inverted nucleobase positioning during product synthesis. We demonstrate that correct nucleotide selection in the CD-NTase donor pocket results in the formation of a thermostable-protein-nucleotide complex, and we extend our analysis to establish specific patterns governing selectivity for each of the major bacterial CD-NTase clades A-H. Our results explain CD-NTase specificity and enable predictions of nucleotide second-messenger signals within diverse antiviral systems.
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Molecular basis of CD-NTase nucleotide selection in CBASS anti-phage defense.,Govande AA, Duncan-Lowey B, Eaglesham JB, Whiteley AT, Kranzusch PJ Cell Rep. 2021 Jun 1;35(9):109206. doi: 10.1016/j.celrep.2021.109206. PMID:34077735<ref>PMID:34077735</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7ljn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bradyrhizobium diazoefficiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Eaglesham, J B]]
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[[Category: Eaglesham JB]]
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[[Category: Govande, A]]
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[[Category: Govande A]]
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[[Category: Kranzusch, P J]]
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[[Category: Kranzusch PJ]]
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[[Category: Lowey, B]]
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[[Category: Lowey B]]
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[[Category: Whiteley, A T]]
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[[Category: Whiteley AT]]
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[[Category: Cbass]]
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[[Category: Cd-ntase]]
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[[Category: Transferase]]
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Current revision

Structure of the Bradyrhizobium diazoefficiens CD-NTase CdnG in complex with GTP

PDB ID 7ljn

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