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4uwm
From Proteopedia
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| - | ''' | + | ==Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.== |
| + | <StructureSection load='4uwm' size='340' side='right' caption='[[4uwm]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4uwm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UWM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UWM FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | ||
| + | <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=4uwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uwm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uwm RCSB], [http://www.ebi.ac.uk/pdbsum/4uwm PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/C16MO_PSEPU C16MO_PSEPU]] Involved in the degradation of (-)-camphor. Catalyzes the lactonization of the 3,6-diketocamphane via the Baeyer-Villiger oxidation to produce the unstable lactone (-)-5-oxo-1,2-campholide that presumably undergoes spontaneous hydrolysis to form 2-oxo-delta(3)-4,5,5-trimethylcyclopentenylacetic acid. It acts only on bicyclic ketones.<ref>PMID:22286514</ref> <ref>PMID:8515237</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The oxygenating constituent of the 3,6-diketocamphane monooxygenase isozyme from Pseudomonas putida NCIMB 10007 has been crystallized under two different conditions. Crystals were initially grown from polyethylene glycol (PEG) 8000 and sodium acetate using the vapour-phase diffusion method. The crystals were of orthorhombic P212121 space group, with cell dimensions a = 55.8, b = 94.5 and c = 163.7 A and diffracted to 2.8 A resolution. More recently, improved crystals, which diffracted beyond 2 A, have been grown from ammonium sulfate. These crystals also belong to the orthorhombic P212121 space group, with cell dimensions of a = 54.6, b = 93.2 and c = 154. 1 A. A full native data set to 2.5 A resolution has been collected from the ammonium sulfate grown crystals. | ||
| - | + | Crystallization and preliminary X-ray diffraction studies of the oxygenating subunit of 3,6-diketocamphane monooxygenase from Pseudomonas putida.,McGhie EJ, Isupov MN, Schroder E, Littlechild JA Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1035-8. PMID:9757131<ref>PMID:9757131</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Beecher, J]] | ||
| + | [[Category: Bornscheuer, U T]] | ||
| + | [[Category: Bourenkov, G]] | ||
| + | [[Category: Davenport, C F]] | ||
| + | [[Category: Dcunha, S]] | ||
[[Category: Donadio, G]] | [[Category: Donadio, G]] | ||
| - | [[Category: | + | [[Category: Gibson, R P]] |
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[[Category: Hasegawa, Y]] | [[Category: Hasegawa, Y]] | ||
| - | [[Category: | + | [[Category: Isupov, M N]] |
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[[Category: Iwaki, H]] | [[Category: Iwaki, H]] | ||
| + | [[Category: Kadow, M]] | ||
| + | [[Category: Lau, P C]] | ||
| + | [[Category: Littlechild, J A]] | ||
[[Category: Loschinski, K]] | [[Category: Loschinski, K]] | ||
| + | [[Category: McGhie, E J]] | ||
| + | [[Category: Saneei, V]] | ||
| + | [[Category: Sayer, C]] | ||
[[Category: Schroeder, E]] | [[Category: Schroeder, E]] | ||
| - | [[Category: | + | [[Category: Biocatalysis]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | + | ||
Revision as of 13:28, 26 August 2015
Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.
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Categories: Beecher, J | Bornscheuer, U T | Bourenkov, G | Davenport, C F | Dcunha, S | Donadio, G | Gibson, R P | Hasegawa, Y | Isupov, M N | Iwaki, H | Kadow, M | Lau, P C | Littlechild, J A | Loschinski, K | McGhie, E J | Saneei, V | Sayer, C | Schroeder, E | Biocatalysis | Oxidoreductase
