1i5a: Difference between revisions
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== | ==STRUCTURE OF CHEA DOMAIN P4 IN COMPLEX WITH ADPCP AND MANGANESE== | ||
[[1i5a]] is a 2 chain structure with sequence from [ | <StructureSection load='1i5a' size='340' side='right'caption='[[1i5a]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1i5a]] is a 2 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=1I5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I5A 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]] 1.9Å</td></tr> | |||
<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=MN:MANGANESE+(II)+ION'>MN</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=1i5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5a OCA], [https://pdbe.org/1i5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i5a RCSB], [https://www.ebi.ac.uk/pdbsum/1i5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5a 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/i5/1i5a_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=1i5a 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 1i5a" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Chemotaxis protein|Chemotaxis protein]] | *[[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]] | ||
Latest revision as of 06:22, 9 August 2023
STRUCTURE OF CHEA DOMAIN P4 IN COMPLEX WITH ADPCP AND MANGANESE
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