3dge: Difference between revisions

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{{Seed}}
[[Image:3dge.png|left|200px]]


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==Structure of a histidine kinase-response regulator complex reveals insights into Two-component signaling and a novel cis-autophosphorylation mechanism==
The line below this paragraph, containing "STRUCTURE_3dge", creates the "Structure Box" on the page.
<StructureSection load='3dge' size='340' side='right'caption='[[3dge]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3dge]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. The October 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Two-component Systems''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_10 10.2210/rcsb_pdb/mom_2015_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DGE FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_3dge|  PDB=3dge  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dge OCA], [https://pdbe.org/3dge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dge RCSB], [https://www.ebi.ac.uk/pdbsum/3dge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dge ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9WYT9_THEMA Q9WYT9_THEMA]
== 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/dg/3dge_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3dge ConSurf].
<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.


===Structure of a histidine kinase-response regulator complex reveals insights into Two-component signaling and a novel cis-autophosphorylation mechanism===
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>
</div>
<div class="pdbe-citations 3dge" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_19800110}}, adds the Publication Abstract to the page
*[[Response regulator 3D structure|Response regulator 3D structure]]
(as it appears on PubMed at http://www.pubmed.gov), where 19800110 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_19800110}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3DGE is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DGE OCA].
[[Category: RCSB PDB Molecule of the Month]]
 
==Reference==
<ref group="xtra">PMID:19800110</ref><references group="xtra"/>
[[Category: Histidine kinase]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Casino, P.]]
[[Category: Two-component Systems]]
[[Category: Marina, A.]]
[[Category: Casino P]]
[[Category: Atp binding domain]]
[[Category: Marina A]]
[[Category: Four-helix bundle]]
[[Category: Kinase]]
[[Category: Phosphoprotein]]
[[Category: Receiver domain]]
[[Category: Transferase]]
[[Category: Transferase/signaling protein complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 21 09:34:09 2009''

Latest revision as of 10:55, 9 October 2024

Structure of a histidine kinase-response regulator complex reveals insights into Two-component signaling and a novel cis-autophosphorylation mechanismStructure of a histidine kinase-response regulator complex reveals insights into Two-component signaling and a novel cis-autophosphorylation mechanism

Structural highlights

3dge is a 4 chain structure with sequence from Thermotoga maritima. The October 2015 RCSB PDB Molecule of the Month feature on Two-component Systems by David Goodsell is 10.2210/rcsb_pdb/mom_2015_10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9WYT9_THEMA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Casino P, Rubio V, Marina A. Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell. 2009 Oct 16;139(2):325-36. Epub 2009 Oct 1. PMID:19800110 doi:10.1016/j.cell.2009.08.032

3dge, resolution 2.80Å

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