3lid: Difference between revisions

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{{STRUCTURE_3lid|  PDB=3lid  |  SCENE=  }}
==Crystal Structure of the extracellular domain of the putative histidine kinase vpHK1S-Z8==
===Crystal Structure of the extracellular domain of the putative histidine kinase vpHK1S-Z8===
<StructureSection load='3lid' size='340' side='right' caption='[[3lid]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
{{ABSTRACT_PUBMED_20435045}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3lid]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LID FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3li8|3li8]], [[3li9|3li9]], [[3lia|3lia]], [[3lib|3lib]], [[3lic|3lic]], [[3lie|3lie]], [[3lif|3lif]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP0354 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=670 Vibrio parahaemolyticus])</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=3lid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lid OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lid RCSB], [http://www.ebi.ac.uk/pdbsum/3lid PDBsum]</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/li/3lid_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histidine kinase (HK) receptors are used ubiquitously by bacteria to monitor environmental changes, and they are also prevalent in plants, fungi, and other protists. Typical HK receptors have an extracellular sensor portion that detects a signal, usually a chemical ligand, and an intracellular transmitter portion that includes both the kinase domain itself and the site for histidine phosphorylation. While kinase domains are highly conserved, sensor domains are diverse. HK receptors function as dimers, but the molecular mechanism for signal transduction across cell membranes remains obscure. In this study, eight crystal structures were determined from five sensor domains representative of the most populated family, family HK1, found in a bioinformatic analysis of predicted sensor domains from transmembrane HKs. Each structure contains an inserted repeat of PhoQ/DcuS/CitA (PDC) domains, and similarity between sequence and structure is correlated across these and other double-PDC sensor proteins. Three of the five sensors crystallize as dimers that appear to be physiologically relevant, and comparisons between ligated structures and apo-state structures provide insights into signal transmission. Some HK1 family proteins prove to be sensors for chemotaxis proteins or diguanylate cyclase receptors, implying a combinatorial molecular evolution.


==About this Structure==
Structural characterization of the predominant family of histidine kinase sensor domains.,Zhang Z, Hendrickson WA J Mol Biol. 2010 Jul 16;400(3):335-53. Epub 2010 May 8. PMID:20435045<ref>PMID:20435045</ref>
[[3lid]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LID OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:020435045</ref><references group="xtra"/><references/>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Vibrio parahaemolyticus]]
[[Category: Vibrio parahaemolyticus]]
[[Category: Hendrickson, W A.]]
[[Category: Hendrickson, W A]]
[[Category: Zhang, Z.]]
[[Category: Zhang, Z]]
[[Category: Pdc fold]]
[[Category: Pdc fold]]
[[Category: Signaling protein]]
[[Category: Signaling protein]]

Revision as of 19:29, 18 December 2014

Crystal Structure of the extracellular domain of the putative histidine kinase vpHK1S-Z8Crystal Structure of the extracellular domain of the putative histidine kinase vpHK1S-Z8

Structural highlights

3lid is a 2 chain structure with sequence from Vibrio parahaemolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:VP0354 (Vibrio parahaemolyticus)
Resources:FirstGlance, OCA, RCSB, PDBsum

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

Histidine kinase (HK) receptors are used ubiquitously by bacteria to monitor environmental changes, and they are also prevalent in plants, fungi, and other protists. Typical HK receptors have an extracellular sensor portion that detects a signal, usually a chemical ligand, and an intracellular transmitter portion that includes both the kinase domain itself and the site for histidine phosphorylation. While kinase domains are highly conserved, sensor domains are diverse. HK receptors function as dimers, but the molecular mechanism for signal transduction across cell membranes remains obscure. In this study, eight crystal structures were determined from five sensor domains representative of the most populated family, family HK1, found in a bioinformatic analysis of predicted sensor domains from transmembrane HKs. Each structure contains an inserted repeat of PhoQ/DcuS/CitA (PDC) domains, and similarity between sequence and structure is correlated across these and other double-PDC sensor proteins. Three of the five sensors crystallize as dimers that appear to be physiologically relevant, and comparisons between ligated structures and apo-state structures provide insights into signal transmission. Some HK1 family proteins prove to be sensors for chemotaxis proteins or diguanylate cyclase receptors, implying a combinatorial molecular evolution.

Structural characterization of the predominant family of histidine kinase sensor domains.,Zhang Z, Hendrickson WA J Mol Biol. 2010 Jul 16;400(3):335-53. Epub 2010 May 8. PMID:20435045[1]

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

References

  1. ↑ Zhang Z, Hendrickson WA. Structural characterization of the predominant family of histidine kinase sensor domains. J Mol Biol. 2010 Jul 16;400(3):335-53. Epub 2010 May 8. PMID:20435045 doi:10.1016/j.jmb.2010.04.049

3lid, resolution 1.76Å

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