3dgf
From Proteopedia
(Difference between revisions)
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<StructureSection load='3dgf' size='340' side='right'caption='[[3dgf]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3dgf' size='340' side='right'caption='[[3dgf]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3dgf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3dgf]] 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=3DGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DGF 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]] 2Å</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=3dgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dgf OCA], [https://pdbe.org/3dgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dgf RCSB], [https://www.ebi.ac.uk/pdbsum/3dgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dgf 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=3dgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dgf OCA], [https://pdbe.org/3dgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dgf RCSB], [https://www.ebi.ac.uk/pdbsum/3dgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dgf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9WYT9_THEMA Q9WYT9_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=3dgf 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=3dgf ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The chief mechanism used by bacteria for sensing their environment is based on two conserved proteins: a sensor histidine kinase (HK) and an effector response regulator (RR). The signal transduction process involves highly conserved domains of both proteins that mediate autokinase, phosphotransfer, and phosphatase activities whose output is a finely tuned RR phosphorylation level. Here, we report the structure of the complex between the entire cytoplasmic portion of Thermotoga maritima class I HK853 and its cognate, RR468, as well as the structure of the isolated RR468, both free and BeF(3)(-) bound. Our results provide insight into partner specificity in two-component systems, recognition of the phosphorylation state of each partner, and the catalytic mechanism of the phosphatase reaction. Biochemical analysis shows that the HK853-catalyzed autokinase reaction proceeds by a cis autophosphorylation mechanism within the HK subunit. The results suggest a model for the signal transduction mechanism in two-component systems. | ||
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| - | Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction.,Casino P, Rubio V, Marina A Cell. 2009 Oct 16;139(2):325-36. Epub 2009 Oct 1. PMID:19800110<ref>PMID:19800110</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3dgf" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Receiver domain of sensor histidine kinase CKI1|Receiver domain of sensor histidine kinase CKI1]] | *[[Receiver domain of sensor histidine kinase CKI1|Receiver domain of sensor histidine kinase CKI1]] | ||
*[[Response regulator 3D structure|Response regulator 3D structure]] | *[[Response regulator 3D structure|Response regulator 3D structure]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 43589]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Thermotoga maritima]] |
| - | [[Category: | + | [[Category: Casino P]] |
| - | [[Category: | + | [[Category: Marina A]] |
| - | + | ||
Current revision
Structure of a histidine kinase-response regulator complex reveals insights into Two-component signaling and a novel cis-autophosphorylation mechanism
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