View source for 7ebl


==Bacterial STING in complex with c-di-GMP==
<StructureSection load='7ebl' size='340' side='right'caption='[[7ebl]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ebl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myroides_sp._ZB35 Myroides sp. ZB35]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EBL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</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=7ebl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ebl OCA], [https://pdbe.org/7ebl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ebl RCSB], [https://www.ebi.ac.uk/pdbsum/7ebl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ebl ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mammalian innate immune sensor STING (STimulator of INterferon Gene) was recently found to originate from bacteria. During phage infection, bacterial STING sense c-di-GMP generated by the CD-NTase (cGAS/DncV-like nucleotidyltransferase) encoded in the same operon and signal suicide commitment as a defense strategy that restricts phage propagation. However, the precise binding mode of c-di-GMP to bacterial STING and the specific recognition mechanism are still elusive. Here, we determine two complex crystal structures of bacterial STING/c-di-GMP, which provide a clear picture of how c-di-GMP is distinguished from other cyclic dinucleotides. The protein-protein interactions further reveal the driving force behind filament formation of bacterial STING. Finally, we group the bacterial STING into two classes based on the conserved motif in beta-strand lid, which dictate their ligand specificity and oligomerization mechanism, and propose an evolution-based model that describes the transition from c-di-GMP-dependent signaling in bacteria to 2'3'-cGAMP-dependent signaling in eukaryotes.

Crystal structure and functional implication of bacterial STING.,Ko TP, Wang YC, Yang CS, Hou MH, Chen CJ, Chiu YF, Chen Y Nat Commun. 2022 Jan 10;13(1):26. doi: 10.1038/s41467-021-26583-3. PMID:35013136<ref>PMID:35013136</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ebl" style="background-color:#fffaf0;"></div>

==See Also==
*[[Stimulator of interferon genes protein 3D structures|Stimulator of interferon genes protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Myroides sp. ZB35]]
[[Category: Chen Y]]
[[Category: Hou M-H]]
[[Category: Ko T-P]]
[[Category: Wang Y-C]]
[[Category: Yang C-S]]