3lnr
From Proteopedia
(Difference between revisions)
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==Crystal structure of poly-HAMP domains from the P. aeruginosa soluble receptor Aer2== | ==Crystal structure of poly-HAMP domains from the P. aeruginosa soluble receptor Aer2== | ||
| - | <StructureSection load='3lnr' size='340' side='right' caption='[[3lnr]], [[Resolution|resolution]] 2.64Å' scene=''> | + | <StructureSection load='3lnr' size='340' side='right'caption='[[3lnr]], [[Resolution|resolution]] 2.64Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3lnr]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3lnr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LNR FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.64Å</td></tr> |
| - | <tr id=' | + | <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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lnr OCA], [https://pdbe.org/3lnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lnr RCSB], [https://www.ebi.ac.uk/pdbsum/3lnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lnr ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == 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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lnr ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lnr ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | HAMP domains are widespread prokaryotic signaling modules found as single domains or poly-HAMP chains in both transmembrane and soluble proteins. The crystal structure of a three-unit poly-HAMP chain from the Pseudomonas aeruginosa soluble receptor Aer2 defines a universal parallel four-helix bundle architecture for diverse HAMP domains. Two contiguous domains integrate to form a concatenated di-HAMP structure. The three HAMP domains display two distinct conformations that differ by changes in helical register, crossing angle, and rotation. These conformations are stabilized by different subsets of conserved residues. Known signals delivered to HAMP would be expected to switch the relative stability of the two conformations and the position of a coiled-coil phase stutter at the junction with downstream helices. We propose that the two conformations represent opposing HAMP signaling states and suggest a signaling mechanism whereby HAMP domains interconvert between the two states, which alternate down a poly-HAMP chain. | ||
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| - | Structure of concatenated HAMP domains provides a mechanism for signal transduction.,Airola MV, Watts KJ, Bilwes AM, Crane BR Structure. 2010 Mar 14;18(4):436-48. PMID:20399181<ref>PMID:20399181</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3lnr" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: | + | [[Category: Airola MV]] |
| - | [[Category: | + | [[Category: Bilwes AM]] |
| - | [[Category: | + | [[Category: Crane BR]] |
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Current revision
Crystal structure of poly-HAMP domains from the P. aeruginosa soluble receptor Aer2
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