3t8y

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==Crystal structure of the response regulator domain of Thermotoga maritima CheB==
==Crystal structure of the response regulator domain of Thermotoga maritima CheB==
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<StructureSection load='3t8y' size='340' side='right' caption='[[3t8y]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='3t8y' size='340' side='right'caption='[[3t8y]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3t8y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T8Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3t8y]] 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=3T8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T8Y FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cheB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-glutamate_methylesterase Protein-glutamate methylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.61 3.1.1.61] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t8y OCA], [https://pdbe.org/3t8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t8y RCSB], [https://www.ebi.ac.uk/pdbsum/3t8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t8y ProSAT]</span></td></tr>
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<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=3t8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t8y OCA], [http://pdbe.org/3t8y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t8y RCSB], [http://www.ebi.ac.uk/pdbsum/3t8y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t8y ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CHEB_THEMA CHEB_THEMA]] Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR (By similarity).
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[https://www.uniprot.org/uniprot/CHEB_THEMA CHEB_THEMA] Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CheA-mediated CheB phosphorylation and the subsequent CheB-mediated demethylation of the chemoreceptors are important steps required for the bacterial chemotactic adaptation response. Although Escherichia coli CheB has been reported to interact with CheA competitively against CheY, we have observed that Thermotoga maritima CheB has no detectable CheA-binding. By determining the CheY-like domain crystal structure of T. maritima CheB, and comparing against the T. maritima CheY and Salmonella typhimurium CheB structures, we propose that the two consecutive glutamates in the beta4/alpha4 loop of T. maritima CheB that is absent in T. maritima CheY and in E. coli/S. typhimurium CheB may be one factor contributing to the low CheA affinity.
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Structural insight into the low affinity between Thermotoga maritima CheA and CheB compared to their Escherichia coli/Salmonella typhimurium counterparts.,Park S, Crane BR Int J Biol Macromol. 2011 Nov 1;49(4):794-800. Epub 2011 Jul 23. PMID:21816169<ref>PMID:21816169</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3t8y" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Chemotaxis protein|Chemotaxis protein]]
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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*[[Response regulator|Response regulator]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43589]]
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[[Category: Large Structures]]
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[[Category: Protein-glutamate methylesterase]]
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[[Category: Thermotoga maritima]]
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[[Category: Crane, B R]]
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[[Category: Crane BR]]
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[[Category: Park, S Y]]
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[[Category: Park SY]]
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[[Category: Chea]]
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[[Category: Hydrolase]]
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[[Category: Response regulator]]
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Current revision

Crystal structure of the response regulator domain of Thermotoga maritima CheB

PDB ID 3t8y

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