5c93: Difference between revisions
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==Histidine kinase with ATP== | ==Histidine kinase with ATP== | ||
<StructureSection load='5c93' size='340' side='right' caption='[[5c93]], [[Resolution|resolution]] 2.52Å' scene=''> | <StructureSection load='5c93' size='340' side='right'caption='[[5c93]], [[Resolution|resolution]] 2.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5c93]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C93 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5c93]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactiplantibacillus_plantarum_16 Lactiplantibacillus plantarum 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C93 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]] 2.518Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5c93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c93 OCA], [https://pdbe.org/5c93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c93 RCSB], [https://www.ebi.ac.uk/pdbsum/5c93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c93 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Lactiplantibacillus plantarum 16]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Cai Y]] | ||
Latest revision as of 19:07, 8 November 2023
Histidine kinase with ATPHistidine kinase with ATP
Structural highlights
Publication Abstract from PubMedTwo-component systems (TCSs) are key elements in bacterial signal transduction in response to environmental stresses. TCSs generally consist of sensor histidine kinases (SKs) and their cognate response regulators (RRs). Many SKs exhibit autokinase, phosphoryltransferase and phosphatase activities, which regulate RR activity through a phosphorylation and dephosphorylation cycle. However, how SKs perform different enzymatic activities is poorly understood. Here, several crystal structures of the minimal catalytic region of WalK, an essential SK from Lactobacillus plantarum that shares 60% sequence identity with its homologue VicK from Streptococcus mutans, are presented. WalK adopts an asymmetrical closed structure in the presence of ATP or ADP, in which one of the CA domains is positioned close to the DHp domain, thus leading both the beta- and gamma-phosphates of ATP/ADP to form hydrogen bonds to the - but not the delta-nitrogen of the phosphorylatable histidine in the DHp domain. In addition, the DHp domain in the ATP/ADP-bound state has a 25.7 degrees asymmetrical helical bending coordinated with the repositioning of the CA domain; these processes are mutually exclusive and alternate in response to helicity changes that are possibly regulated by upstream signals. In the absence of ATP or ADP, however, WalK adopts a completely symmetric open structure with its DHp domain centred between two outward-reaching CA domains. In summary, these structures of WalK reveal the intrinsic dynamic properties of an SK structure as a molecular basis for multifunctionality. Conformational dynamics of the essential sensor histidine kinase WalK.,Cai Y, Su M, Ahmad A, Hu X, Sang J, Kong L, Chen X, Wang C, Shuai J, Han A Acta Crystallogr D Struct Biol. 2017 Oct 1;73(Pt 10):793-803. doi:, 10.1107/S2059798317013043. Epub 2017 Sep 27. PMID:28994408[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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