1oyb: Difference between revisions

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 <StructureSection load='1oyb' size='340' side='right'caption='[[1oyb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1oyb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_2.2402 As 2.2402]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OYB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1oyb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_pastorianus Saccharomyces pastorianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OYB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=HBA:P-HYDROXYBENZALDEHYDE'>HBA</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]] 2&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OYE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=27292 AS 2.2402])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=HBA:P-HYDROXYBENZALDEHYDE'>HBA</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADPH_dehydrogenase NADPH dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.1 1.6.99.1] </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=1oyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oyb OCA], [https://pdbe.org/1oyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oyb RCSB], [https://www.ebi.ac.uk/pdbsum/1oyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oyb ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1oyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oyb OCA], [http://pdbe.org/1oyb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oyb RCSB], [http://www.ebi.ac.uk/pdbsum/1oyb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oyb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/OYE1_SACPS OYE1_SACPS]] Oxidizes beta-NADH, beta-NADPH, and alpha-NADPH.
+[https://www.uniprot.org/uniprot/OYE1_SACPS OYE1_SACPS] Oxidizes beta-NADH, beta-NADPH, and alpha-NADPH.
 == 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=1oyb ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-BACKGROUND: Old yellow enzyme (OYE) was the first flavoenzyme purified, but its function is still unknown. Nevertheless, the NADPH oxidase activity, the flavin mononucleotide environment and the ligand-binding properties of OYE have been extensively studied by biochemical and spectroscopic approaches. Full interpretation of these data requires structural information. RESULTS: The crystal structures of oxidized and reduced OYE at 2 A resolution reveal an alpha/beta-barrel topology clearly related to trimethylamine dehydrogenase. Complexes of OYE with p-hydroxybenzaldehyde, beta-estradiol, and an NADPH analog show all three binding at a common site, stacked on the flavin. The putative NADPH binding mode is novel as it involves primary recognition of the nicotinamide mononucleotide portion. CONCLUSIONS: This work shows that the striking spectral changes seen upon phenol binding are due to close physical association of the flavin and phenolate. It also identifies the structural class of OYE and suggests that if NADPH is its true substrate, then OYE has adopted NADPH dependence during evolution.
-Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins.,Fox KM, Karplus PA Structure. 1994 Nov 15;2(11):1089-105. PMID:7881908<ref>PMID:7881908</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1oyb" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[NADPH dehydrogenase|NADPH dehydrogenase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: As 2 2402]]
 [[Category: Large Structures]]
-[[Category: NADPH dehydrogenase]]
+[[Category: Saccharomyces pastorianus]]
-[[Category: Fox, K M]]
+[[Category: Fox KM]]
-[[Category: Karplus, P A]]
+[[Category: Karplus PA]]