7k5n
From Proteopedia
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==Ligand binding domain (tandem PAS/dCache) of Aeromonas caviae diguanylate cyclase with proline bound== | ==Ligand binding domain (tandem PAS/dCache) of Aeromonas caviae diguanylate cyclase with proline bound== | ||
- | <StructureSection load='7k5n' size='340' side='right'caption='[[7k5n]]' scene=''> | + | <StructureSection load='7k5n' size='340' side='right'caption='[[7k5n]], [[Resolution|resolution]] 1.80Å' 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=7K5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K5N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7k5n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_caviae Aeromonas caviae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K5N 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=7k5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k5n OCA], [https://pdbe.org/7k5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k5n RCSB], [https://www.ebi.ac.uk/pdbsum/7k5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k5n ProSAT]</span></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]] 1.8Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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=7k5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k5n OCA], [https://pdbe.org/7k5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k5n RCSB], [https://www.ebi.ac.uk/pdbsum/7k5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k5n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/A0A3S5WQC2_AERCA A0A3S5WQC2_AERCA] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Animal microbiomes are assembled predominantly from environmental microbes, yet the mechanisms by which individual symbionts regulate their transmission into hosts remain underexplored. By tracking the experimental evolution of Aeromonas veronii in gnotobiotic zebrafish, we identify bacterial traits promoting host colonization. Multiple independently evolved isolates with increased immigration harbored mutations in a gene we named sensor of proline diguanylate cyclase enzyme (SpdE) based on structural, biochemical, and phenotypic evidence that SpdE encodes an amino-acid-sensing diguanylate cyclase. SpdE detects free proline and to a lesser extent valine and isoleucine, resulting in reduced production of intracellular c-di-GMP, a second messenger controlling bacterial motility. Indeed, SpdE binding to amino acids increased bacterial motility and host colonization. Hosts serve as sources of SpdE-detected amino acids, with levels varying based on microbial colonization status. Our work demonstrates that bacteria use chemically regulated motility, or chemokinesis, to sense host-emitted cues that trigger active immigration into hosts. | ||
+ | |||
+ | Host-emitted amino acid cues regulate bacterial chemokinesis to enhance colonization.,Robinson CD, Sweeney EG, Ngo J, Ma E, Perkins A, Smith TJ, Fernandez NL, Waters CM, Remington SJ, Bohannan BJM, Guillemin K Cell Host Microbe. 2021 Aug 11;29(8):1221-1234.e8. doi:, 10.1016/j.chom.2021.06.003. Epub 2021 Jul 6. PMID:34233153<ref>PMID:34233153</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7k5n" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Diguanylate cyclase|Diguanylate cyclase]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Aeromonas caviae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Remington SJ]] | [[Category: Remington SJ]] | ||
[[Category: Sweeney EG]] | [[Category: Sweeney EG]] |
Current revision
Ligand binding domain (tandem PAS/dCache) of Aeromonas caviae diguanylate cyclase with proline bound
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