6rh1: Difference between revisions
New page: '''Unreleased structure''' The entry 6rh1 is ON HOLD Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Revisiting pH-gated conformational switch. Complex HK853-RR468 D53A pH 7== | |||
<StructureSection load='6rh1' size='340' side='right'caption='[[6rh1]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rh1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RH1 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<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=6rh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rh1 OCA], [https://pdbe.org/6rh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rh1 RCSB], [https://www.ebi.ac.uk/pdbsum/6rh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rh1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9WZV7_THEMA Q9WZV7_THEMA] | |||
<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 6rh1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Response regulator 3D structure|Response regulator 3D structure]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermotoga maritima]] | |||
[[Category: Casino P]] | |||
[[Category: Marina A]] | |||
[[Category: Mideros-Mora C]] | |||
Latest revision as of 15:20, 24 January 2024
Revisiting pH-gated conformational switch. Complex HK853-RR468 D53A pH 7Revisiting pH-gated conformational switch. Complex HK853-RR468 D53A pH 7
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
|
| ||||||||||||||||||