4i44
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4i44]] 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=4I44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I44 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4i44]] 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=4I44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I44 FirstGlance]. <br> | ||
| - | </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></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]] 2.88Å</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></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=4i44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i44 OCA], [https://pdbe.org/4i44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i44 RCSB], [https://www.ebi.ac.uk/pdbsum/4i44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i44 ProSAT]</span></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=4i44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i44 OCA], [https://pdbe.org/4i44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i44 RCSB], [https://www.ebi.ac.uk/pdbsum/4i44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i44 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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> | [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> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4i44" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Aer2 poly-HAMP domains: V33G HAMP1 inverted signaling mutant
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