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| <StructureSection load='6mi6' size='340' side='right'caption='[[6mi6]], [[Resolution|resolution]] 2.95Å' scene=''> | | <StructureSection load='6mi6' size='340' side='right'caption='[[6mi6]], [[Resolution|resolution]] 2.95Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6mi6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MI6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mi6]] is a 4 chain structure with sequence from [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=6MI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MI6 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=JSJ:5-O-[(S)-hydroxy{[(S)-hydroxy{[(1-hydroxy-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl]disulfanyl}phosphoryl]oxy}phosphoryl]adenosine'>JSJ</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]] 2.95Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cheA, TM_0702 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=JSJ:[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-[(2,2,5,5-tetramethyl-1-oxidanyl-pyrrol-3-yl)methyldisulfanyl]phosphinic+acid'>JSJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></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=6mi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mi6 OCA], [https://pdbe.org/6mi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mi6 RCSB], [https://www.ebi.ac.uk/pdbsum/6mi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mi6 ProSAT]</span></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=6mi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mi6 OCA], [http://pdbe.org/6mi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mi6 RCSB], [http://www.ebi.ac.uk/pdbsum/6mi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mi6 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/CHEA_THEMA CHEA_THEMA]] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY (By similarity). | + | [https://www.uniprot.org/uniprot/CHEA_THEMA CHEA_THEMA] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY (By similarity). |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Histidine kinase]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Thema]] | + | [[Category: Thermotoga maritima MSB8]] |
- | [[Category: Chua, T K]] | + | [[Category: Chua TK]] |
- | [[Category: Crane, B R]] | + | [[Category: Crane BR]] |
- | [[Category: Le, H]] | + | [[Category: Le H]] |
- | [[Category: Muok, A R]] | + | [[Category: Muok AR]] |
- | [[Category: Bacterial chemotaxis]]
| + | |
- | [[Category: Signaling protein]]
| + | |
- | [[Category: Thermotoga maritima]]
| + | |
| Structural highlights
Function
CHEA_THEMA Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY (By similarity).
Publication Abstract from PubMed
Site-directed spin labeling of proteins by chemical modification of engineered cysteine residues with the molecule MTSSL (1-Oxyl-2,2,5,5-tetramethylpyrroline-3-methyl methanethiosulfonate) has been an invaluable tool for conducting double electron electron resonance (DEER) spectroscopy experiments. However, this method is generally limited to recombinant proteins with a limited number of reactive Cys residues that when modified will not impair protein function. Here we present a method that allows for spin-labeling of protein nucleotide binding sites by adenosine diphosphate (ADP) modified with a nitroxide moiety on the beta-phosphate (ADP-beta-S-SL). The synthesis of this ADP analog is straightforward and isolation of pure product is readily achieved on a standard reverse-phase high-performance liquid chromatography (HPLC) system. Furthermore, analyses of isolated ADP-beta-S-SL by LC-mass spectrometry confirm that the molecule is extremely stable under ambient conditions. The crystal structure of ADP-beta-S-SL bound to the ATP pocket of the histidine kinase CheA reveals specific targeting of the probe, whose nitroxide moiety is mobile on the protein surface. Continuous wave and pulsed ESR measurements demonstrate the capability of ADP-beta-S-SL to report on active site environment and provide reliable DEER distance constraints.
Nucleotide Spin Labeling for ESR Spectroscopy of ATP-Binding Proteins.,Muok AR, Chua TK, Le H, Crane BR Appl Magn Reson. 2018 Dec;49(12):1385-1395. doi: 10.1007/s00723-018-1070-6. Epub , 2018 Nov 14. PMID:30686862[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Muok AR, Chua TK, Le H, Crane BR. Nucleotide Spin Labeling for ESR Spectroscopy of ATP-Binding Proteins. Appl Magn Reson. 2018 Dec;49(12):1385-1395. doi: 10.1007/s00723-018-1070-6. Epub , 2018 Nov 14. PMID:30686862 doi:http://dx.doi.org/10.1007/s00723-018-1070-6
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