6dsp
From Proteopedia
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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=6dsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dsp OCA], [http://pdbe.org/6dsp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dsp RCSB], [http://www.ebi.ac.uk/pdbsum/6dsp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dsp ProSAT]</span></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=6dsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dsp OCA], [http://pdbe.org/6dsp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dsp RCSB], [http://www.ebi.ac.uk/pdbsum/6dsp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dsp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Autoinducer-2 (AI-2) is unique among quorum-sensing signaling molecules, as it is produced and recognized by a wide variety of bacteria and thus facilitates interspecies communication. To date, two classes of AI-2 receptors have been identified: the LuxP-type, present in the Vibrionales, and the LsrB-type, found in a number of phylogenetically distinct bacterial families. Recently, AI-2 was shown to affect the colonization levels of a variety of bacteria in the microbiome of the mouse gut, including members of the genus Clostridium, but no AI-2 receptor had been identified in this genus. Here, we identify a noncanonical, functional LsrB-type receptor in Clostridium saccharobutylicum. This novel LsrB-like receptor is the first one reported with variations in the binding-site amino acid residues that interact with AI-2. The crystal structure of the C. saccharobutylicum receptor determined at 1.35 A resolution revealed that it binds the same form of AI-2 as the other known LsrB-type receptors, and isothermal titration calorimetry (ITC) assays showed that binding of AI-2 occurs at a submicromolar concentration. Using phylogenetic analysis, we inferred that the newly identified noncanonical LsrB receptor shares a common ancestor with known LsrB receptors and that noncanonical receptors are present in bacteria from different phyla. This led us to identify putative AI-2 receptors in bacterial species in which no receptors were known, as in bacteria belonging to the Spirochaetes and Actinobacteria phyla. Thus, this work represents a significant step toward understanding how AI-2-mediated quorum sensing influences bacterial interactions in complex biological niches. | ||
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| + | Identification of novel autoinducer-2 receptors in Clostridia reveals plasticity in the binding site of the LsrB receptor family.,Torcato IM, Kasal MR, Brito PH, Miller ST, Xavier KB J Biol Chem. 2019 Mar 22;294(12):4450-4463. doi: 10.1074/jbc.RA118.006938. Epub, 2019 Jan 29. PMID:30696769<ref>PMID:30696769</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6dsp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:26, 21 August 2019
LsrB from Clostridium saccharobutylicum in complex with AI-2
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