6sy9: Difference between revisions
New page: '''Unreleased structure''' The entry 6sy9 is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Structure of the Legionella pneumophila response regulator LqsR== | ||
<StructureSection load='6sy9' size='340' side='right'caption='[[6sy9]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6sy9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33152 Atcc 33152]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SY9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SY9 FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C3926_14995, C3927_13800, D7214_05345, ERS240541_01816, ERS253249_00465, NCTC12000_02932 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=446 ATCC 33152])</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=6sy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sy9 OCA], [http://pdbe.org/6sy9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sy9 RCSB], [http://www.ebi.ac.uk/pdbsum/6sy9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sy9 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The water-borne bacterium Legionella pneumophila replicates in environmental protozoa and upon inhalation destroys alveolar macrophages, thus causing a potentially fatal pneumonia termed 'Legionnaires' disease'. L. pneumophila employs the Legionella quorum sensing (Lqs) system to control its life cycle, pathogen-host cell interactions, motility and natural competence. Signaling through the Lqs system occurs through the alpha-hydroxyketone compound Legionella autoinducer-1 (LAI-1) and converges on the prototypic response regulator LqsR, which dimerizes upon phosphorylation of the conserved aspartate, D108 . In this study, we determine the high-resolution structure of monomeric LqsR. The structure reveals a receiver domain adopting a canonical (betaalpha)5 fold, which is connected through an additional sixth helix and an extended alpha5-helix to a novel output domain. The two domains delineate a mainly positively charged groove, and the output domain adopts a five-stranded antiparallel beta-sheet fold similar to nucleotide-binding proteins. Structure-based mutagenesis identified amino acids critical for LqsR phosphorylation and dimerization. Upon phosphorylation, the LqsRD172A and LqsRD302N/E303Q mutant proteins dimerized even more readily than wild-type LqsR, and no evidence for semi-phosphorylated heterodimers was obtained. Taken together, the high-resolution structure of LqsR reveals functionally relevant amino acid residues implicated in signal transduction of the prototypic response regulator. | |||
The structure of the Legionella response regulator LqsR reveals amino acids critical for phosphorylation and dimerization.,Hochstrasser R, Hutter CAJ, Arnold FM, Barlocher K, Seeger MA, Hilbi H Mol Microbiol. 2020 Jan 29. doi: 10.1111/mmi.14477. PMID:31997467<ref>PMID:31997467</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6sy9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Atcc 33152]] | |||
[[Category: Large Structures]] | |||
[[Category: Arnold, F M]] | |||
[[Category: Baerlocher, K]] | |||
[[Category: Hilbi, H]] | |||
[[Category: Hochstrasser, R]] | |||
[[Category: Hutter, C A.J]] | |||
[[Category: Seeger, M A]] | |||
[[Category: Output domain]] | |||
[[Category: Receiver domain]] | |||
[[Category: Response regulator]] | |||
[[Category: Signaling protein]] | |||
Latest revision as of 10:34, 19 February 2020
Structure of the Legionella pneumophila response regulator LqsRStructure of the Legionella pneumophila response regulator LqsR
Structural highlights
Publication Abstract from PubMedThe water-borne bacterium Legionella pneumophila replicates in environmental protozoa and upon inhalation destroys alveolar macrophages, thus causing a potentially fatal pneumonia termed 'Legionnaires' disease'. L. pneumophila employs the Legionella quorum sensing (Lqs) system to control its life cycle, pathogen-host cell interactions, motility and natural competence. Signaling through the Lqs system occurs through the alpha-hydroxyketone compound Legionella autoinducer-1 (LAI-1) and converges on the prototypic response regulator LqsR, which dimerizes upon phosphorylation of the conserved aspartate, D108 . In this study, we determine the high-resolution structure of monomeric LqsR. The structure reveals a receiver domain adopting a canonical (betaalpha)5 fold, which is connected through an additional sixth helix and an extended alpha5-helix to a novel output domain. The two domains delineate a mainly positively charged groove, and the output domain adopts a five-stranded antiparallel beta-sheet fold similar to nucleotide-binding proteins. Structure-based mutagenesis identified amino acids critical for LqsR phosphorylation and dimerization. Upon phosphorylation, the LqsRD172A and LqsRD302N/E303Q mutant proteins dimerized even more readily than wild-type LqsR, and no evidence for semi-phosphorylated heterodimers was obtained. Taken together, the high-resolution structure of LqsR reveals functionally relevant amino acid residues implicated in signal transduction of the prototypic response regulator. The structure of the Legionella response regulator LqsR reveals amino acids critical for phosphorylation and dimerization.,Hochstrasser R, Hutter CAJ, Arnold FM, Barlocher K, Seeger MA, Hilbi H Mol Microbiol. 2020 Jan 29. doi: 10.1111/mmi.14477. PMID:31997467[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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