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{{STRUCTURE_3kpx|  PDB=3kpx  |  SCENE=  }}
===Crystal Structure Analysis of photoprotein clytin===
{{ABSTRACT_PUBMED_20926380}}


==About this Structure==
==Crystal Structure Analysis of photoprotein clytin==
[[3kpx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clytia_gregaria Clytia gregaria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KPX OCA].  
<StructureSection load='3kpx' size='340' side='right'caption='[[3kpx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3kpx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clytia_gregaria Clytia gregaria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KPX 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]] 1.899&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CZH:C2-HYDROPEROXY-COELENTERAZINE'>CZH</scene></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=3kpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kpx OCA], [https://pdbe.org/3kpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kpx RCSB], [https://www.ebi.ac.uk/pdbsum/3kpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kpx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D7PM14_CLYGR D7PM14_CLYGR]
== 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/kp/3kpx_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=3kpx ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Forster resonance energy transfer within a protein-protein complex has previously been invoked to explain emission spectral modulation observed in several bioluminescence systems. Here we present a spatial structure of a complex of the Ca(2+)-regulated photoprotein clytin with its green-fluorescent protein (cgGFP) from the jellyfish Clytia gregaria, and show that it accounts for the bioluminescence properties of this system in vitro. We adopted an indirect approach of combining x-ray crystallography determined structures of the separate proteins, NMR spectroscopy, computational docking, and mutagenesis. Heteronuclear NMR spectroscopy using variously (15)N,(13)C,(2)H-enriched proteins enabled assignment of backbone resonances of more than 94% of the residues of both proteins. In a mixture of the two proteins at millimolar concentrations, complexation was inferred from perturbations of certain (1)H-(15)N HSQC-resonances, which could be mapped to those residues involved at the interaction site. A docking computation using HADDOCK was employed constrained by the sites of interaction, to deduce an overall spatial structure of the complex. Contacts within the clytin-cgGFP complex and electrostatic complementarity of interaction surfaces argued for a weak protein-protein complex. A weak affinity was also observed by isothermal titration calorimetry (K(D) = 0.9 mm). Mutation of clytin residues located at the interaction site reduced the degree of protein-protein association concomitant with a loss of effectiveness of cgGFP in color-shifting the bioluminescence. It is suggested that this clytin-cgGFP structure corresponds to the transient complex previously postulated to account for the energy transfer effect of GFP in the bioluminescence of aequorin or Renilla luciferase.


==Reference==
NMR-derived Topology of a GFP-photoprotein Energy Transfer Complex.,Titushin MS, Feng Y, Stepanyuk GA, Li Y, Markova SV, Golz S, Wang BC, Lee J, Wang J, Vysotski ES, Liu ZJ J Biol Chem. 2010 Dec 24;285(52):40891-900. Epub 2010 Oct 6. PMID:20926380<ref>PMID:20926380</ref>
<ref group="xtra">PMID:020926380</ref><references group="xtra"/><references/>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3kpx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clytia gregaria]]
[[Category: Clytia gregaria]]
[[Category: Renilla-luciferin 2-monooxygenase]]
[[Category: Large Structures]]
[[Category: Lee, J.]]
[[Category: Lee J]]
[[Category: Li, Y.]]
[[Category: Li Y]]
[[Category: Liu, Z J.]]
[[Category: Liu Z-J]]
[[Category: Stepanyuk, G A.]]
[[Category: Stepanyuk GA]]
[[Category: Titushin, M S.]]
[[Category: Titushin MS]]
[[Category: Vysotski, E S.]]
[[Category: Vysotski ES]]
[[Category: Wang, B C.]]
[[Category: Wang B-C]]
[[Category: Fluorescent protein]]
[[Category: Hydrolase]]
[[Category: Photoprotein clytin]]