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[[Image:2pse.gif|left|200px]]<br /><applet load="2pse" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2pse, resolution 2.50&Aring;" />
'''Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla Reniformis'''<br />


==Overview==
==Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla Reniformis==
Due to its ability to emit light, the luciferase from Renilla reniformis, (RLuc) is widely employed in molecular biology as a reporter gene in cell, culture experiments and small animal imaging. To accomplish this, bioluminescence, the 37-kDa enzyme catalyzes the degradation of its, substrate coelenterazine in the presence of molecular oxygen, resulting in, the product coelenteramide, carbon dioxide, and the desired photon of, light. We successfully crystallized a stabilized variant of this important, protein (RLuc8) and herein present the first structures for any, coelenterazine-using luciferase. These structures are based on, high-resolution data measured to 1.4 A and demonstrate a classic, alpha/beta-hydrolase fold. We also present data of a coelenteramide-bound, luciferase and reason that this structure represents a secondary, conformational form following shift of the product out of the primary, active site. During the course of this work, the structure of the, luciferase's accessory green fluorescent protein (RrGFP) was also, determined and shown to be highly similar to that of Aequorea victoria, GFP.
<StructureSection load='2pse' size='340' side='right'caption='[[2pse]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2pse]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Renilla_reniformis Renilla reniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PSE 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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=2pse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pse OCA], [https://pdbe.org/2pse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pse RCSB], [https://www.ebi.ac.uk/pdbsum/2pse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pse ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LUCI_RENRE LUCI_RENRE]
== 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/ps/2pse_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=2pse ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2PSE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Renilla_reniformis Renilla reniformis] with <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Renilla-luciferin_2-monooxygenase Renilla-luciferin 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.5 1.13.12.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PSE OCA].
*[[Luciferase 3D structures|Luciferase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis., Loening AM, Fenn TD, Gambhir SS, J Mol Biol. 2007 Dec 7;374(4):1017-28. Epub 2007 Oct 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17980388 17980388]
[[Category: Large Structures]]
[[Category: Renilla reniformis]]
[[Category: Renilla reniformis]]
[[Category: Renilla-luciferin 2-monooxygenase]]
[[Category: Fenn TD]]
[[Category: Single protein]]
[[Category: Gambhir SS]]
[[Category: Fenn, T.D.]]
[[Category: Loening AM]]
[[Category: Gambhir, S.S.]]
[[Category: Loening, A.M.]]
[[Category: IMD]]
[[Category: alpha/beta-hydrolase]]
[[Category: luciferase]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:57:03 2008''

Latest revision as of 12:11, 21 February 2024

Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla ReniformisCrystal Structures of the Luciferase and Green Fluorescent Protein from Renilla Reniformis

Structural highlights

2pse is a 1 chain structure with sequence from Renilla reniformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LUCI_RENRE

Evolutionary Conservation

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

See Also

2pse, resolution 2.50Å

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