7ljl
From Proteopedia
(Difference between revisions)
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==Structure of the Enterobacter cloacae CD-NTase CdnD in complex with ATP== | ==Structure of the Enterobacter cloacae CD-NTase CdnD in complex with ATP== | ||
| - | <StructureSection load='7ljl' size='340' side='right'caption='[[7ljl]]' scene=''> | + | <StructureSection load='7ljl' size='340' side='right'caption='[[7ljl]], [[Resolution|resolution]] 1.45Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LJL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ljl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"aerobacter_cloacae"_(jordan_1890)_bergey_et_al._1923 "aerobacter cloacae" (jordan 1890) bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LJL FirstGlance]. <br> |
| - | </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=7ljl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ljl OCA], [https://pdbe.org/7ljl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ljl RCSB], [https://www.ebi.ac.uk/pdbsum/7ljl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ljl ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cdnD02, P853_02262 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=550 "Aerobacter cloacae" (Jordan 1890) Bergey et al. 1923])</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=7ljl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ljl OCA], [https://pdbe.org/7ljl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ljl RCSB], [https://www.ebi.ac.uk/pdbsum/7ljl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ljl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/CDND2_ENTCL CDND2_ENTCL]] CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-C(AAG) CBASS system (PubMed:32839535).<ref>PMID:32544385</ref> <ref>PMID:32839535</ref> Cyclic trinucleotide synthase that catalyzes the synthesis of 3',3',3'-cyclic AMP-AMP-GMP as the major product, a second messenger for cell signal transduction.<ref>PMID:30787435</ref> Protects E.coli against phage T2 infection. When the cdnD-cap2-cap3-cap4 operon is introduced in E.coli there is a more than 10(3) decrease in the efficiency of T2 plaque formation. The operon does not protect against phage T5 and only about 10-fold against T7.<ref>PMID:32544385</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ljl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Eaglesham | + | [[Category: Eaglesham, J B]] |
| - | [[Category: Govande A]] | + | [[Category: Govande, A]] |
| - | [[Category: Kranzusch | + | [[Category: Kranzusch, P J]] |
| - | [[Category: Lowey B]] | + | [[Category: Lowey, B]] |
| - | [[Category: Whiteley | + | [[Category: Whiteley, A W]] |
| + | [[Category: Cbass]] | ||
| + | [[Category: Cd-ntase]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Trinucleotide]] | ||
Revision as of 10:10, 14 July 2021
Structure of the Enterobacter cloacae CD-NTase CdnD in complex with ATP
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