4uwm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='4uwm' size='340' side='right'caption='[[4uwm]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4uwm' size='340' side='right'caption='[[4uwm]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4uwm]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4uwm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. 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 [https://proteopedia.org/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> | </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=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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uwm OCA], [https://pdbe.org/4uwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uwm RCSB], [https://www.ebi.ac.uk/pdbsum/4uwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uwm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/36DKM_PSEPU 36DKM_PSEPU] Involved in the degradation and assimilation of (-)-camphor, which allows P.putida strain NCIMB 10007 to grow on this enantiomer of camphor as the sole carbon source (PubMed:8515237). Catalyzes the FMNH(2)-dependent lactonization of 3,6-diketocamphane via a Baeyer-Villiger oxidation to produce the unstable lactone 5-oxo-1,2-campholide with (S,S) configuration, that presumably undergoes spontaneous hydrolysis to form 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetate (PubMed:23524667). Is also able to convert (-)-camphor to the corresponding lactone in vitro (PubMed:23524667, PubMed:22286514, PubMed:8515237). Shows no conversion of (+)-camphor, (+)-fenchone, (-)-fenchone, and (+)-nopinone. Acts on other bicyclic ketones but very poorly on a few 2- and 4-substituted monocyclic ketones (PubMed:23524667).<ref>PMID:22286514</ref> <ref>PMID:23524667</ref> <ref>PMID:8515237</ref> <ref>PMID:8515237</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 25: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Beecher | [[Category: Pseudomonas putida]] | ||
[[Category: Bornscheuer | [[Category: Beecher J]] | ||
[[Category: Bourenkov | [[Category: Bornscheuer UT]] | ||
[[Category: Davenport | [[Category: Bourenkov G]] | ||
[[Category: Dcunha | [[Category: Davenport CF]] | ||
[[Category: Donadio | [[Category: Dcunha S]] | ||
[[Category: Gibson | [[Category: Donadio G]] | ||
[[Category: Hasegawa | [[Category: Gibson RP]] | ||
[[Category: Isupov | [[Category: Hasegawa Y]] | ||
[[Category: Iwaki | [[Category: Isupov MN]] | ||
[[Category: Kadow | [[Category: Iwaki H]] | ||
[[Category: Lau | [[Category: Kadow M]] | ||
[[Category: Littlechild | [[Category: Lau PC]] | ||
[[Category: Loschinski | [[Category: Littlechild JA]] | ||
[[Category: McGhie | [[Category: Loschinski K]] | ||
[[Category: Saneei | [[Category: McGhie EJ]] | ||
[[Category: Sayer | [[Category: Saneei V]] | ||
[[Category: Schroeder | [[Category: Sayer C]] | ||
[[Category: Schroeder E]] | |||
Revision as of 10:48, 29 March 2023
Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.
Structural highlights
Function36DKM_PSEPU Involved in the degradation and assimilation of (-)-camphor, which allows P.putida strain NCIMB 10007 to grow on this enantiomer of camphor as the sole carbon source (PubMed:8515237). Catalyzes the FMNH(2)-dependent lactonization of 3,6-diketocamphane via a Baeyer-Villiger oxidation to produce the unstable lactone 5-oxo-1,2-campholide with (S,S) configuration, that presumably undergoes spontaneous hydrolysis to form 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetate (PubMed:23524667). Is also able to convert (-)-camphor to the corresponding lactone in vitro (PubMed:23524667, PubMed:22286514, PubMed:8515237). Shows no conversion of (+)-camphor, (+)-fenchone, (-)-fenchone, and (+)-nopinone. Acts on other bicyclic ketones but very poorly on a few 2- and 4-substituted monocyclic ketones (PubMed:23524667).[1] [2] [3] [4] Publication Abstract from PubMedThe three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer-Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 A resolution. The structure of this dimeric FMN-dependent enzyme, which is encoded on the large CAM plasmid of Pseudomonas putida, has been solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model. The orientation of the isoalloxazine ring of the FMN cofactor in the active site of this TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in a cis conformation and forms a beta-bulge at the C-terminus of beta-strand 3, which is a feature observed in many proteins of this superfamily. The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer-Villiger monooxygenase.,Isupov MN, Schroder E, Gibson RP, Beecher J, Donadio G, Saneei V, Dcunha SA, McGhie EJ, Sayer C, Davenport CF, Lau PC, Hasegawa Y, Iwaki H, Kadow M, Balke K, Bornscheuer UT, Bourenkov G, Littlechild JA Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2344-53. doi:, 10.1107/S1399004715017939. Epub 2015 Oct 31. PMID:26527149[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||