6rh8: Difference between revisions
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==Revisiting pH-gated conformational switch. Complex HK853 mutant H260A -RR468 mutant D53A pH 5.3== | |||
<StructureSection load='6rh8' size='340' side='right'caption='[[6rh8]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== 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 [http://oca.weizmann.ac.il/oca-docs/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> | |||
<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=6rh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rh8 OCA], [http://pdbe.org/6rh8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rh8 RCSB], [http://www.ebi.ac.uk/pdbsum/6rh8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rh8 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Histidine 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<ref>PMID:32034139</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6rh8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Casino, P]] | |||
[[Category: Marina, A]] | |||
[[Category: Mideros-Mora, C]] | |||
[[Category: Histidine kinase]] | |||
[[Category: Phosphatase]] | |||
[[Category: Phosphotransfer]] | |||
[[Category: Response regulator]] | |||
[[Category: Signaling protein]] | |||
Revision as of 09:32, 19 February 2020
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
Publication 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. References
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