View source for 3gl9


==The structure of a histidine kinase-response regulator complex sheds light into two-component signaling and reveals a novel cis autophosphorylation mechanism==
<StructureSection load='3gl9' size='340' side='right' caption='[[3gl9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3gl9]] is a 4 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=3GL9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GL9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene></td></tr>
<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=3gl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gl9 OCA], [http://pdbe.org/3gl9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gl9 RCSB], [http://www.ebi.ac.uk/pdbsum/3gl9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gl9 ProSAT]</span></td></tr>
</table>
== 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/gl/3gl9_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=3gl9 ConSurf].
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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3gl9" style="background-color:#fffaf0;"></div>

==See Also==
*[[Response regulator|Response regulator]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 43589]]
[[Category: Casino, P]]
[[Category: Marina, A]]
[[Category: Rubio, V]]
[[Category: Beta-sheet]]
[[Category: Both side]]
[[Category: Signaling protein]]
[[Category: Surrounded by alpha helice]]