6e0k

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Current revision (14:38, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6e0k' size='340' side='right'caption='[[6e0k]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='6e0k' size='340' side='right'caption='[[6e0k]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6e0k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhomg Rhomg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E0K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E0K FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6e0k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodothermus_marinus_SG0.5JP17-172 Rhodothermus marinus SG0.5JP17-172]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E0K FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rhom172_2837 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=762570 RHOMG])</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='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=6e0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0k OCA], [http://pdbe.org/6e0k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e0k RCSB], [http://www.ebi.ac.uk/pdbsum/6e0k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0k ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6e0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0k OCA], [https://pdbe.org/6e0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e0k RCSB], [https://www.ebi.ac.uk/pdbsum/6e0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0k 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/CDNE_RHOMG CDNE_RHOMG] 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 I-B(UU) CBASS system (PubMed:32839535).<ref>PMID:32839535</ref> Cyclic dinucleotide synthase that catalyzes the synthesis of 3'3'-cyclic UMP-AMP (cUMP-AMP) from UTP and ATP, a second messenger for cell signal transduction.<ref>PMID:30787435</ref>
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Cyclic dinucleotides (CDNs) have central roles in bacterial homeostasis and virulence by acting as nucleotide second messengers. Bacterial CDNs also elicit immune responses during infection when they are detected by pattern-recognition receptors in animal cells. Here we perform a systematic biochemical screen for bacterial signalling nucleotides and discover a large family of cGAS/DncV-like nucleotidyltransferases (CD-NTases) that use both purine and pyrimidine nucleotides to synthesize a diverse range of CDNs. A series of crystal structures establish CD-NTases as a structurally conserved family and reveal key contacts in the enzyme active-site lid that direct purine or pyrimidine selection. CD-NTase products are not restricted to CDNs and also include an unexpected class of cyclic trinucleotide compounds. Biochemical and cellular analyses of CD-NTase signalling nucleotides demonstrate that these cyclic di- and trinucleotides activate distinct host receptors and thus may modulate the interaction of both pathogens and commensal microbiota with their animal and plant hosts.
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Bacterial cGAS-like enzymes synthesize diverse nucleotide signals.,Whiteley AT, Eaglesham JB, de Oliveira Mann CC, Morehouse BR, Lowey B, Nieminen EA, Danilchanka O, King DS, Lee ASY, Mekalanos JJ, Kranzusch PJ Nature. 2019 Feb 20. pii: 10.1038/s41586-019-0953-5. doi:, 10.1038/s41586-019-0953-5. PMID:30787435<ref>PMID:30787435</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 6e0k" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Rhomg]]
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[[Category: Rhodothermus marinus SG0 5JP17-172]]
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[[Category: Eaglesham, J B]]
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[[Category: Eaglesham JB]]
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[[Category: King, D S]]
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[[Category: King DS]]
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[[Category: Kranzusch, P J]]
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[[Category: Kranzusch PJ]]
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[[Category: Lee, A S.Y]]
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[[Category: Lee ASY]]
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[[Category: Mann, C C.de Oliveira]]
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[[Category: Mekalanos JJ]]
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[[Category: Mekalanos, J J]]
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[[Category: Morehouse BR]]
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[[Category: Morehouse, B R]]
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[[Category: Nieminen EA]]
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[[Category: Nieminen, E A]]
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[[Category: Whiteley AT]]
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[[Category: Whiteley, A T]]
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[[Category: De Oliveira Mann CC]]
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[[Category: Cga]]
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[[Category: Cyclic dinucleotide]]
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[[Category: Dncv]]
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[[Category: Nucleotide second messenger]]
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[[Category: Nucleotidyltransferase]]
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[[Category: Transferase]]
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Current revision

Structure of Rhodothermus marinus CdnE c-UMP-AMP synthase

PDB ID 6e0k

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Proteopedia Page Contributors and Editors (what is this?)

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