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3g6b
From Proteopedia
(Difference between revisions)
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<StructureSection load='3g6b' size='340' side='right'caption='[[3g6b]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='3g6b' size='340' side='right'caption='[[3g6b]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3g6b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3g6b]] 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=3G6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G6B 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]] 3Å</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=3g6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g6b OCA], [https://pdbe.org/3g6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g6b RCSB], [https://www.ebi.ac.uk/pdbsum/3g6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g6b ProSAT]</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=3g6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g6b OCA], [https://pdbe.org/3g6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g6b RCSB], [https://www.ebi.ac.uk/pdbsum/3g6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g6b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q7DFA3_THEMA Q7DFA3_THEMA] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=3g6b ConSurf]. | </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=3g6b ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Transmembrane chemoreceptors, also known as methyl-accepting chemotaxis proteins (MCPs), translate extracellular signals into intracellular responses in the bacterial chemotaxis system. MCP ligand binding domains control the activity of the CheA kinase, situated approximately 200 A away, across the cytoplasmic membrane. The 2.17 A resolution crystal structure of a Thermotoga maritima soluble receptor (Tm14) reveals distortions in its dimeric four-helix bundle that provide insight into the conformational states available to MCPs for propagating signals. A bulge in one helix generates asymmetry between subunits that displaces the kinase-interacting tip, which resides more than 100 A away. The maximum bundle distortion maps to the adaptation region of transmembrane MCPs where reversible methylation of acidic residues tunes receptor activity. Minor alterations in coiled-coil packing geometry translate the bulge distortion to a >25 A movement of the tip relative to the bundle stalks. The Tm14 structure discloses how alterations in local helical structure, which could be induced by changes in methylation state and/or by conformational signals from membrane proximal regions, can reposition a remote domain that interacts with the CheA kinase. | ||
| - | |||
| - | The structure of a soluble chemoreceptor suggests a mechanism for propagating conformational signals.,Pollard AM, Bilwes AM, Crane BR Biochemistry. 2009 Mar 10;48(9):1936-44. PMID:19149470<ref>PMID:19149470</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3g6b" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | ||
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | *[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 43589]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Thermotoga maritima]] |
| - | [[Category: | + | [[Category: Bilwes AM]] |
| - | [[Category: | + | [[Category: Crane BR]] |
| - | [[Category: | + | [[Category: Pollard AM]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of a Soluble Chemoreceptor from Thermotoga maritima Asn217Ile mutant
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