6e0n: Difference between revisions

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<StructureSection load='6e0n' size='340' side='right'caption='[[6e0n]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='6e0n' size='340' side='right'caption='[[6e0n]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6e0n]] 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=6E0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E0N FirstGlance]. <br>
<table><tr><td colspan='2'>[[6e0n]] 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=6E0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E0N FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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=6e0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0n OCA], [http://pdbe.org/6e0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e0n RCSB], [http://www.ebi.ac.uk/pdbsum/6e0n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0n ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <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=6e0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0n OCA], [https://pdbe.org/6e0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e0n RCSB], [https://www.ebi.ac.uk/pdbsum/6e0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0n ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0A4V8GZR7_ELIME A0A4V8GZR7_ELIME]
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6e0n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 13253]]
[[Category: Elizabethkingia meningoseptica ATCC 13253 = NBRC 12535]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Eaglesham, J B]]
[[Category: Eaglesham JB]]
[[Category: King, D S]]
[[Category: King DS]]
[[Category: Kranzusch, P J]]
[[Category: Kranzusch PJ]]
[[Category: Lee, A S.Y]]
[[Category: Lee ASY]]
[[Category: Mann, C C.de Oliveira]]
[[Category: Mekalanos JJ]]
[[Category: Mekalanos, J J]]
[[Category: Morehouse BR]]
[[Category: Morehouse, B R]]
[[Category: Nieminen EA]]
[[Category: Nieminen, E A]]
[[Category: Whiteley AT]]
[[Category: Whiteley, A T]]
[[Category: De Oliveira Mann CC]]
[[Category: Cga]]
[[Category: Cyclic dinucleotide]]
[[Category: Dncv]]
[[Category: Nucleotide second messenger]]
[[Category: Nucleotidyltransferase]]
[[Category: Transferase]]
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