6rh8: Difference between revisions
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<StructureSection load='6rh8' size='340' side='right'caption='[[6rh8]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6rh8' size='340' side='right'caption='[[6rh8]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6rh8]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RH8 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6rh8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] and [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RH8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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]] 1.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6rh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rh8 OCA], [https://pdbe.org/6rh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rh8 RCSB], [https://www.ebi.ac.uk/pdbsum/6rh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rh8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9WZV7_THEMA Q9WZV7_THEMA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6rh8" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6rh8" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Response regulator 3D structure|Response regulator 3D structure]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima]] | ||
[[Category: | [[Category: Thermotoga maritima MSB8]] | ||
[[Category: | [[Category: Casino P]] | ||
[[Category: | [[Category: Marina A]] | ||
[[Category: | [[Category: Mideros-Mora C]] | ||
Latest revision as of 15:20, 24 January 2024
Revisiting pH-gated conformational switch. Complex HK853 mutant H260A -RR468 mutant D53A pH 5.3Revisiting pH-gated conformational switch. Complex HK853 mutant H260A -RR468 mutant D53A pH 5.3
Structural highlights
FunctionPublication Abstract from PubMedHistidine is a versatile residue playing key roles in enzyme catalysis thanks to the chemistry of its imidazole group that can serve as nucleophile, general acid or base depending on its protonation state. In bacteria, signal transduction relies on two-component systems (TCS) which comprise a sensor histidine kinase (HK) containing a phosphorylatable catalytic His with phosphotransfer and phosphatase activities over an effector response regulator. Recently, a pH-gated model has been postulated to regulate the phosphatase activity of HisKA HKs based on the pH-dependent rotamer switch of the phosphorylatable His. Here, we have revisited this model from a structural and functional perspective on HK853-RR468 and EnvZ-OmpR TCS, the prototypical HisKA HKs. We have found that the rotamer of His is not influenced by the environmental pH, ruling out a pH-gated model and confirming that the chemistry of the His is responsible for the decrease in the phosphatase activity at acidic pH. Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases.,Mideros-Mora C, Miguel-Romero L, Felipe-Ruiz A, Casino P, Marina A Nat Commun. 2020 Feb 7;11(1):769. doi: 10.1038/s41467-020-14540-5. PMID:32034139[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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