1m5t: Difference between revisions

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New page: left|200px<br /><applet load="1m5t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5t, resolution 1.60Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1m5t.jpg|left|200px]]<br /><applet load="1m5t" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1m5t, resolution 1.60&Aring;" />
'''CRYSTAL STRUCTURE OF THE RESPONSE REGULATOR DIVK'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE RESPONSE REGULATOR DIVK==
DivK is an essential response regulator in the Gram-negative bacterium, Caulobacter crescentus and functions in a complex phosphorelay system that, precisely controls the sequence of developmental events during the cell, division cycle. Structure determinations of this single domain response, regulator at different pH values demonstrated that the five-stranded, alpha/beta fold of the DivK protein is fully defined only at acidic pH., The crystal structures of the apoprotein and of metal-bound DivK complexes, at higher pH values revealed a synergistic pH- and cation binding-induced, flexibility of the beta4-alpha4 loop and of the alpha4 helix. This motion, increases the solvent accessibility of the single cysteine residue in the, protein. Solution state studies demonstrated a 200-fold pH-dependent, increase in the affinity of manganese for the protein between pH 6.0 and, 8.5 that seems to involve deprotonation of an acido-basic couple. Taken, together, these results suggest that flexibility of critical regions of, the protein, ionization of the cysteine 99 residue and improved K(D), values for the catalytic metal ion are coupled events. We propose that the, molecular events observed in the isolated protein may be required for DivK, activation and that they may be achieved in vivo through the specific, protein-protein interactions between the response regulator and its, cognate kinases.
<StructureSection load='1m5t' size='340' side='right'caption='[[1m5t]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1m5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M5T FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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=1m5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5t OCA], [https://pdbe.org/1m5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m5t RCSB], [https://www.ebi.ac.uk/pdbsum/1m5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m5t ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9A5I4_CAUVC Q9A5I4_CAUVC]
== 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/m5/1m5t_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=1m5t ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1M5T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M5T OCA].
*[[Response regulator 3D structure|Response regulator 3D structure]]
 
__TOC__
==Reference==
</StructureSection>
Crystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentus., Guillet V, Ohta N, Cabantous S, Newton A, Samama JP, J Biol Chem. 2002 Nov 1;277(44):42003-10. Epub 2002 Aug 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12176983 12176983]
[[Category: Caulobacter vibrioides]]
[[Category: Caulobacter vibrioides]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cabantous, S.]]
[[Category: Cabantous S]]
[[Category: Guillet, V.]]
[[Category: Guillet V]]
[[Category: Newton, A.]]
[[Category: Newton A]]
[[Category: Ohta, N.]]
[[Category: Ohta N]]
[[Category: SPINE, Structural.Proteomics.in.Europe.]]
[[Category: Samama J-P]]
[[Category: Samama, J.P.]]
[[Category: response regulator]]
[[Category: signal transduction protein]]
[[Category: spine]]
[[Category: structural genomics]]
[[Category: structural proteomics in europe]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:49:01 2007''

Latest revision as of 10:40, 14 February 2024

CRYSTAL STRUCTURE OF THE RESPONSE REGULATOR DIVKCRYSTAL STRUCTURE OF THE RESPONSE REGULATOR DIVK

Structural highlights

1m5t is a 1 chain structure with sequence from Caulobacter vibrioides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9A5I4_CAUVC

Evolutionary Conservation

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

See Also

1m5t, resolution 1.60Å

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