1i5d
From Proteopedia
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| - | {{STRUCTURE_1i5d| PDB=1i5d | SCENE= }} | ||
| - | ===STRUCTURE OF CHEA DOMAIN P4 IN COMPLEX WITH TNP-ATP=== | ||
| - | {{ABSTRACT_PUBMED_11276258}} | ||
| - | == | + | ==STRUCTURE OF CHEA DOMAIN P4 IN COMPLEX WITH TNP-ATP== |
| - | [[1i5d]] is a 1 chain structure with sequence from [ | + | <StructureSection load='1i5d' size='340' side='right'caption='[[1i5d]], [[Resolution|resolution]] 2.90Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1i5d]] is a 1 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=1I5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I5D 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]] 2.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=128:SPIRO(2,4,6-TRINITROBENZENE[1,2A]-2O,3O-METHYLENE-ADENINE-TRIPHOSPHATE'>128</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=1i5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5d OCA], [https://pdbe.org/1i5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i5d RCSB], [https://www.ebi.ac.uk/pdbsum/1i5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5d ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i5/1i5d_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i5d ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | To probe the structural basis for protein histidine kinase (PHK) catalytic activity and the prospects for PHK-specific inhibitor design, we report the crystal structures for the nucleotide binding domain of Thermotoga maritima CheA with ADP and three ATP analogs (ADPNP, ADPCP and TNP-ATP) bound with either Mg(2+) or Mn(2+). The conformation of ADPNP bound to CheA and related ATPases differs from that reported in the ADPNP complex of PHK EnvZ. Interactions of the active site with the nucleotide gamma-phosphate and its associated Mg(2+) ion are linked to conformational changes in an ATP-lid that could mediate recognition of the substrate domain. The inhibitor TNP-ATP binds CheA with its phosphates in a nonproductive conformation and its adenine and trinitrophenyl groups in two adjacent binding pockets. The trinitrophenyl interaction may be exploited for designing CheA-targeted drugs that would not interfere with host ATPases. | ||
| - | + | Nucleotide binding by the histidine kinase CheA.,Bilwes AM, Quezada CM, Croal LR, Crane BR, Simon MI Nat Struct Biol. 2001 Apr;8(4):353-60. PMID:11276258<ref>PMID:11276258</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| + | <div class="pdbe-citations 1i5d" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Bilwes | + | [[Category: Bilwes AM]] |
| - | [[Category: Crane | + | [[Category: Crane BR]] |
| - | [[Category: Croal | + | [[Category: Croal LR]] |
| - | [[Category: Quezada | + | [[Category: Quezada CM]] |
| - | [[Category: Simon | + | [[Category: Simon MI]] |
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Current revision
STRUCTURE OF CHEA DOMAIN P4 IN COMPLEX WITH TNP-ATP
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