2wht: Difference between revisions

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[[Image:2wht.png|left|200px]]
==Fluorescent Protein mKeima at pH 5.6==
<StructureSection load='2wht' size='340' side='right' caption='[[2wht]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wht]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Montipora_sp._20 Montipora sp. 20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WHT OCA]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRQ:[2-(3-CARBAMOYL-1-IMINO-PROPYL)-4-(4-HYDROXY-BENZYLIDENE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETIC+ACID'>CRQ</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2whu|2whu]], [[2whs|2whs]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wht RCSB], [http://www.ebi.ac.uk/pdbsum/2wht 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/wh/2wht_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 ==
The recently developed red fluorescent protein Keima exhibits the largest Stokes shift (180 nm) observed to date. Combining X-ray crystallography with (in crystallo) UV-visible absorption, fluorescence, and Raman spectroscopy, we have investigated molecular determinants of this peculiar property. The results demonstrate a pH-dependent "reverse chromophore protonation" triggered by the key residue Asp157 and which couples to cis/trans isomerization of the chromophore. These data provided guidelines to rationally design a useful Keima variant.


{{STRUCTURE_2wht|  PDB=2wht  |  SCENE=  }}
Reverse pH-dependence of chromophore protonation explains the large Stokes shift of the red fluorescent protein mKeima.,Violot S, Carpentier P, Blanchoin L, Bourgeois D J Am Chem Soc. 2009 Aug 5;131(30):10356-7. PMID:19722611<ref>PMID:19722611</ref>


===Fluorescent Protein mKeima at pH 5.6===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_19722611}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2wht]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Montipora_sp._20 Montipora sp. 20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WHT OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:019722611</ref><references group="xtra"/>
[[Category: Montipora sp. 20]]
[[Category: Montipora sp. 20]]
[[Category: Blanchoin, L.]]
[[Category: Blanchoin, L.]]

Revision as of 08:30, 7 May 2014

Fluorescent Protein mKeima at pH 5.6

2wht, resolution 1.90Å

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