2psd
From Proteopedia
(Difference between revisions)
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<StructureSection load='2psd' size='340' side='right'caption='[[2psd]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='2psd' size='340' side='right'caption='[[2psd]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2psd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2psd]] 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=2PSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PSD FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</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=' | + | |
- | + | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2psd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2psd OCA], [https://pdbe.org/2psd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2psd RCSB], [https://www.ebi.ac.uk/pdbsum/2psd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2psd ProSAT]</span></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=2psd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2psd OCA], [https://pdbe.org/2psd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2psd RCSB], [https://www.ebi.ac.uk/pdbsum/2psd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2psd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/LUCI_RENRE LUCI_RENRE] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=2psd ConSurf]. | </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=2psd ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 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. | ||
- | |||
- | 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:17980388<ref>PMID:17980388</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2psd" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Luciferase 3D structures|Luciferase 3D structures]] | *[[Luciferase 3D structures|Luciferase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Renilla reniformis]] |
- | + | [[Category: Fenn TD]] | |
- | [[Category: Fenn | + | [[Category: Gambhir SS]] |
- | [[Category: Gambhir | + | [[Category: Loening AM]] |
- | [[Category: Loening | + | |
- | + | ||
- | + | ||
- | + |
Current revision
Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla Reniformis
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