6e0m

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Current revision (14:38, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6e0m' size='340' side='right'caption='[[6e0m]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
<StructureSection load='6e0m' size='340' side='right'caption='[[6e0m]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6e0m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13253 Atcc 13253]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E0M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E0M FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6e0m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica_ATCC_13253_=_NBRC_12535 Elizabethkingia meningoseptica ATCC 13253 = NBRC 12535]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E0M FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</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]] 1.52&#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=6e0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0m OCA], [http://pdbe.org/6e0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e0m RCSB], [http://www.ebi.ac.uk/pdbsum/6e0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0m ProSAT]</span></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=DPO:DIPHOSPHATE'>DPO</scene></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=6e0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0m OCA], [https://pdbe.org/6e0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e0m RCSB], [https://www.ebi.ac.uk/pdbsum/6e0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0m 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_ELIME CDNE_ELIME] 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-A(GA) CBASS system (PubMed:32839535).<ref>PMID:32839535</ref> Cyclic dinucleotide synthase that catalyzes the synthesis of 3'3'-cyclic GMP-AMP (cGAMP) from GTP and ATP, and of c-di-AMP and c-di-GMP, that are second messengers 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 6e0m" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 13253]]
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[[Category: Elizabethkingia meningoseptica ATCC 13253 = NBRC 12535]]
[[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: 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 Elizabethkingia meningoseptica CdnE cyclic dinucleotide synthase

PDB ID 6e0m

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