1luc: Difference between revisions

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 <StructureSection load='1luc' size='340' side='right'caption='[[1luc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1luc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"achromobacter_harveyi"_johnson_and_shunk_1936 "achromobacter harveyi" johnson and shunk 1936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LUC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1luc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LUC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alkanal_monooxygenase_(FMN-linked) Alkanal monooxygenase (FMN-linked)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.3 1.14.14.3] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1luc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1luc OCA], [https://pdbe.org/1luc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1luc RCSB], [https://www.ebi.ac.uk/pdbsum/1luc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1luc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/LUXA_VIBHA LUXA_VIBHA]] Light-emitting reaction in luminous bacteria. [[https://www.uniprot.org/uniprot/LUXB_VIBHA LUXB_VIBHA]] Light-emitting reaction in luminous bacteria. The specific role of the beta subunit is unknown, but it is absolutely required for bioluminescence activity.
+[https://www.uniprot.org/uniprot/LUXA_VIBHA LUXA_VIBHA] Light-emitting reaction in luminous bacteria.
 == Evolutionary Conservation ==
 [[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=1luc ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Bacterial luciferase is a flavin monooxygenase that catalyzes the oxidation of a long-chain aldehyde and releases energy in the form of visible light. A new crystal form of luciferase cloned from Vibrio harveyi has been grown under low-salt concentrations, which diffract x-rays beyond 1.5-A resolution. The x-ray structure of bacterial luciferase has been refined to a conventional R-factor of 18.2% for all recorded synchrotron data between 30.0 and 1.50-A resolution. Bacterial luciferase is an alpha-beta heterodimer, and the individual subunits fold into a single domain (beta/alpha)8 barrel. The high resolution structure reveals a non-prolyl cis peptide bond that forms between Ala74 and Ala75 in the alpha subunit near the putative active site. This cis peptide bond may have functional significance for creating a cavity at the active site. Bacterial luciferase employs reduced flavin as a substrate rather than a cofactor. The structure presented was determined in the absence of substrates. A comparison of the structural similarities between luciferase and a nonfluorescent flavoprotein, which is expressed in the lux operon of one genus of bioluminescent bacteria, suggests that the two proteins originated from a common ancestor. However, the flavin binding sites of the nonfluorescent protein are likely not representative of the flavin binding site on luciferase. The structure presented here will furnish a detailed molecular model for all bacterial luciferases.
-The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions.,Fisher AJ, Thompson TB, Thoden JB, Baldwin TO, Rayment I J Biol Chem. 1996 Sep 6;271(36):21956-68. PMID:8703001<ref>PMID:8703001</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1luc" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Luciferase 3D structures|Luciferase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Achromobacter harveyi johnson and shunk 1936]]
 [[Category: Large Structures]]
-[[Category: Fisher, A J]]
+[[Category: Vibrio harveyi]]
-[[Category: Rayment, I]]
+[[Category: Fisher AJ]]
-[[Category: Flavoprotein]]
+[[Category: Rayment I]]
-[[Category: Monooxygenase]]