2psf: Difference between revisions
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<StructureSection load='2psf' size='340' side='right'caption='[[2psf]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='2psf' size='340' side='right'caption='[[2psf]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2psf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2psf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pennatula_reniformis Pennatula reniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PSF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PSF FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2psd|2psd]], [[2pse|2pse]], [[2psh|2psh]], [[2psj|2psj]], [[2psl|2psl]]</div></td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2psd|2psd]], [[2pse|2pse]], [[2psh|2psh]], [[2psj|2psj]], [[2psl|2psl]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rluc ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6136 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rluc ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6136 Pennatula reniformis])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Renilla-luciferin_2-monooxygenase Renilla-luciferin 2-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.5 1.13.12.5] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Renilla-luciferin_2-monooxygenase Renilla-luciferin 2-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.5 1.13.12.5] </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=2psf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2psf OCA], [https://pdbe.org/2psf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2psf RCSB], [https://www.ebi.ac.uk/pdbsum/2psf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2psf 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=2psf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2psf OCA], [https://pdbe.org/2psf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2psf RCSB], [https://www.ebi.ac.uk/pdbsum/2psf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2psf ProSAT]</span></td></tr> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pennatula reniformis]] | |||
[[Category: Renilla-luciferin 2-monooxygenase]] | [[Category: Renilla-luciferin 2-monooxygenase]] | ||
[[Category: Fenn, T D]] | [[Category: Fenn, T D]] | ||
[[Category: Gambhir, S S]] | [[Category: Gambhir, S S]] | ||
Revision as of 21:28, 20 October 2021
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
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDue 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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