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| ==Aer2 poly-HAMP domains: L44H HAMP1 CW-lock mutant== | | ==Aer2 poly-HAMP domains: L44H HAMP1 CW-lock mutant== |
- | <StructureSection load='4i3m' size='340' side='right' caption='[[4i3m]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='4i3m' size='340' side='right'caption='[[4i3m]], [[Resolution|resolution]] 1.95Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4i3m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I3M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I3M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4i3m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I3M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I3M FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.95Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lnr|3lnr]], [[4i44|4i44]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aer2, PA0176 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</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=4i3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3m OCA], [https://pdbe.org/4i3m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i3m RCSB], [https://www.ebi.ac.uk/pdbsum/4i3m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i3m 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=4i3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i3m RCSB], [http://www.ebi.ac.uk/pdbsum/4i3m PDBsum]</span></td></tr> | + | |
| </table> | | </table> |
- | <div style="background-color:#fffaf0;">
| + | == Function == |
- | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/MCPB_PSEAE MCPB_PSEAE] Chemoreceptor that plays a critical role in the virulence and pathogenesis of P.aeruginosa in a variety of hosts (PubMed:31511598). Probably acts through oxygen sensing (PubMed:31511598, PubMed:28167524, PubMed:34383467). Uses a heme-based sensor (PubMed:21255112, PubMed:22622145). Could be involved in chemotaxis (PubMed:12142407, PubMed:14987771). When expressed in E.coli, is able to sense and mediate repellent responses to oxygen, carbon monoxide and nitric oxide (PubMed:21255112).<ref>PMID:12142407</ref> <ref>PMID:14987771</ref> <ref>PMID:21255112</ref> <ref>PMID:22622145</ref> <ref>PMID:28167524</ref> <ref>PMID:31511598</ref> <ref>PMID:34383467</ref> |
- | HAMP domains are signal relay modules in >26,000 receptors of bacteria, eukaryotes, and archaea that mediate processes involved in chemotaxis, pathogenesis, and biofilm formation. We identify two HAMP conformations distinguished by a four- to two-helix packing transition at the C-termini that send opposing signals in bacterial chemoreceptors. Crystal structures of signal-locked mutants establish the observed structure-to-function relationships. Pulsed dipolar electron spin resonance spectroscopy of spin-labeled soluble receptors active in cells verify that the crystallographically defined HAMP conformers are maintained in the receptors and influence the structure and activity of downstream domains accordingly. Mutation of HR2, a key residue for setting the HAMP conformation and generating an inhibitory signal, shifts HAMP structure and receptor output to an activating state. Another HR2 variant displays an inverted response with respect to ligand and demonstrates the fine energetic balance between "on" and "off" conformers. A DExG motif found in membrane proximal HAMP domains is shown to be critical for responses to extracellular ligand. Our findings directly correlate in vivo signaling with HAMP structure, stability, and dynamics to establish a comprehensive model for HAMP-mediated signal relay that consolidates existing views on how conformational signals propagate in receptors. Moreover, we have developed a rational means to manipulate HAMP structure and function that may prove useful in the engineering of bacterial taxis responses.
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- | HAMP Domain Conformers That Propagate Opposite Signals in Bacterial Chemoreceptors.,Airola MV, Sukomon N, Samanta D, Borbat PP, Freed JH, Watts KJ, Crane BR PLoS Biol. 2013 Feb;11(2):e1001479. doi: 10.1371/journal.pbio.1001479. Epub 2013 , Feb 12. PMID:23424282<ref>PMID:23424282</ref>
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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- | </div> | + | |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| + | [[Category: Large Structures]] |
| [[Category: Pseudomonas aeruginosa]] | | [[Category: Pseudomonas aeruginosa]] |
- | [[Category: Airola, M V]] | + | [[Category: Airola MV]] |
- | [[Category: Crane, B R]] | + | [[Category: Crane BR]] |
- | [[Category: Sukomon, N]] | + | [[Category: Sukomon N]] |
- | [[Category: Hamp domain]]
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- | [[Category: Poly-hamp domain]]
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- | [[Category: Signal relay]]
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- | [[Category: Signal transduction]]
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- | [[Category: Signaling protein]]
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| Structural highlights
Function
MCPB_PSEAE Chemoreceptor that plays a critical role in the virulence and pathogenesis of P.aeruginosa in a variety of hosts (PubMed:31511598). Probably acts through oxygen sensing (PubMed:31511598, PubMed:28167524, PubMed:34383467). Uses a heme-based sensor (PubMed:21255112, PubMed:22622145). Could be involved in chemotaxis (PubMed:12142407, PubMed:14987771). When expressed in E.coli, is able to sense and mediate repellent responses to oxygen, carbon monoxide and nitric oxide (PubMed:21255112).[1] [2] [3] [4] [5] [6] [7]
References
- ↑ Ferrandez A, Hawkins AC, Summerfield DT, Harwood CS. Cluster II che genes from Pseudomonas aeruginosa are required for an optimal chemotactic response. J Bacteriol. 2002 Aug;184(16):4374-83. PMID:12142407
- ↑ Hong CS, Shitashiro M, Kuroda A, Ikeda T, Takiguchi N, Ohtake H, Kato J. Chemotaxis proteins and transducers for aerotaxis in Pseudomonas aeruginosa. FEMS Microbiol Lett. 2004 Feb 16;231(2):247-52. doi:, 10.1016/S0378-1097(04)00009-6. PMID:14987771 doi:http://dx.doi.org/10.1016/S0378-1097(04)00009-6
- ↑ Watts KJ, Taylor BL, Johnson MS. PAS/poly-HAMP signalling in Aer-2, a soluble haem-based sensor. Mol Microbiol. 2011 Feb;79(3):686-99. doi: 10.1111/j.1365-2958.2010.07477.x. Epub, 2010 Dec 7. PMID:21255112 doi:http://dx.doi.org/10.1111/j.1365-2958.2010.07477.x
- ↑ Sawai H, Sugimoto H, Shiro Y, Ishikawa H, Mizutani Y, Aono S. Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa. Chem Commun (Camb). 2012 Jul 4;48(52):6523-5. doi: 10.1039/c2cc32549g. Epub 2012 , May 23. PMID:22622145 doi:10.1039/c2cc32549g
- ↑ Garcia D, Orillard E, Johnson MS, Watts KJ. Gas Sensing and Signaling in the PAS-Heme Domain of the Pseudomonas aeruginosa Aer2 Receptor. J Bacteriol. 2017 Aug 22;199(18). pii: JB.00003-17. doi: 10.1128/JB.00003-17., Print 2017 Sep 15. PMID:28167524 doi:http://dx.doi.org/10.1128/JB.00003-17
- ↑ Garcia-Fontana C, Vilchez JI, Gonzalez-Requena M, Gonzalez-Lopez J, Krell T, Matilla MA, Manzanera M. The involvement of McpB chemoreceptor from Pseudomonas aeruginosa PAO1 in virulence. Sci Rep. 2019 Sep 11;9(1):13166. doi: 10.1038/s41598-019-49697-7. PMID:31511598 doi:http://dx.doi.org/10.1038/s41598-019-49697-7
- ↑ Orillard E, Anaya S, Johnson MS, Watts KJ. Oxygen-Induced Conformational Changes in the PAS-Heme Domain of the Pseudomonas aeruginosa Aer2 Receptor. Biochemistry. 2021 Aug 31;60(34):2610-2622. doi: 10.1021/acs.biochem.1c00452., Epub 2021 Aug 12. PMID:34383467 doi:http://dx.doi.org/10.1021/acs.biochem.1c00452
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