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4g36

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<StructureSection load='4g36' size='340' side='right'caption='[[4g36]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
<StructureSection load='4g36' size='340' side='right'caption='[[4g36]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4g36]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_eastern_firefly Common eastern firefly]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G36 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4g36]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Photinus_pyralis Photinus pyralis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G36 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SLU:5-O-[N-(DEHYDROLUCIFERYL)-SULFAMOYL]+ADENOSINE'>SLU</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.624&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lci|1lci]], [[3iep|3iep]], [[2d1s|2d1s]], [[4g37|4g37]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SLU:5-O-[N-(DEHYDROLUCIFERYL)-SULFAMOYL]+ADENOSINE'>SLU</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Photinus-luciferin_4-monooxygenase_(ATP-hydrolyzing) Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.7 1.13.12.7] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4g36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g36 OCA], [https://pdbe.org/4g36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g36 RCSB], [https://www.ebi.ac.uk/pdbsum/4g36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g36 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g36 OCA], [http://pdbe.org/4g36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g36 RCSB], [http://www.ebi.ac.uk/pdbsum/4g36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g36 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/LUCI_PHOPY LUCI_PHOPY]] Produces green light with a wavelength of 562 nm.
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[https://www.uniprot.org/uniprot/LUCI_PHOPY LUCI_PHOPY] Produces green light with a wavelength of 562 nm.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Beetle luciferases catalyze a two-step reaction that includes the initial adenylation of the luciferin substrate, followed by an oxidative decarboxylation that ultimately produces light. Evidence for homologous acyl-CoA synthetases supports a domain alternation catalytic mechanism in which these enzymes' C-terminal domain rotates by approximately 140 degrees to adopt two conformations that are used to catalyze the two partial reactions. While many structures exist of acyl-CoA synthetases in both conformations, to date only biochemical evidence supports domain alternation with luciferase. We have determined the structure of a cross-linked luciferase enzyme that is trapped in the second conformation. This new structure supports the role of the second catalytic conformation and provides insights into the biochemical mechanism of the luciferase oxidative step.
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Crystal Structure of Firefly Luciferase in a Second Catalytic Conformation Supports a Domain Alternation Mechanism.,Sundlov JA, Fontaine DM, Southworth TL, Branchini BR, Gulick AM Biochemistry. 2012 Aug 6. PMID:22852753<ref>PMID:22852753</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4g36" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Luciferase|Luciferase]]
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*[[Luciferase 3D structures|Luciferase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Common eastern firefly]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Branchini, B R]]
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[[Category: Photinus pyralis]]
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[[Category: Gulick, A M]]
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[[Category: Branchini BR]]
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[[Category: Sundlov, J A]]
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[[Category: Gulick AM]]
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[[Category: Adenylating enzyme]]
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[[Category: Sundlov JA]]
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[[Category: Anl superfamily]]
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[[Category: Domain alternation]]
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[[Category: Firefly luciferase]]
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[[Category: Ligase]]
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[[Category: Luciferase]]
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Current revision

Photinus pyralis luciferase in the adenylate-forming conformation bound to DLSA

PDB ID 4g36

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