5aec

From Proteopedia

(Difference between revisions)

Current revision

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

5aec is a 2 chain structure with sequence from Pseudomonas putida. This structure supersedes the now removed PDB entry 2wgk. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.93Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

The 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.

References

↑ Kadow M, Loschinski K, Sass S, Schmidt M, Bornscheuer UT. Completing the series of BVMOs involved in camphor metabolism of Pseudomonas putida NCIMB 10007 by identification of the two missing genes, their functional expression in E. coli, and biochemical characterization. Appl Microbiol Biotechnol. 2012 Oct;96(2):419-29. PMID:22286514 doi:http://dx.doi.org/10.1007/s00253-011-3859-1
↑ Iwaki H, Grosse S, Bergeron H, Leisch H, Morley K, Hasegawa Y, Lau PC. Camphor pathway redux: functional recombinant expression of 2,5 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions. Appl Environ Microbiol. 2013 May;79(10):3282-93. PMID:23524667 doi:10.1128/AEM.03958-12
↑ Jones KH, Smith RT, Trudgill PW. Diketocamphane enantiomer-specific 'Baeyer-Villiger' monooxygenases from camphor-grown Pseudomonas putida ATCC 17453. J Gen Microbiol. 1993 Apr;139(4):797-805. PMID:8515237
↑ Jones KH, Smith RT, Trudgill PW. Diketocamphane enantiomer-specific 'Baeyer-Villiger' monooxygenases from camphor-grown Pseudomonas putida ATCC 17453. J Gen Microbiol. 1993 Apr;139(4):797-805. PMID:8515237
↑ 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. 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. Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2344-53. doi:, 10.1107/S1399004715017939. Epub 2015 Oct 31. PMID:26527149 doi:http://dx.doi.org/10.1107/S1399004715017939

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5aec"

@@ Line 1: / Line 1: @@
 ==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='5aec' size='340' side='right' caption='[[5aec]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
+<StructureSection load='5aec' size='340' side='right'caption='[[5aec]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5aec]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wgk 2wgk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AEC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5aec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wgk 2wgk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AEC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PIN:PIPERAZINE-N,N-BIS(2-ETHANESULFONIC+ACID)'>PIN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.93&#8491;</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=5aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aec OCA], [http://pdbe.org/5aec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aec RCSB], [http://www.ebi.ac.uk/pdbsum/5aec PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PIN:PIPERAZINE-N,N-BIS(2-ETHANESULFONIC+ACID)'>PIN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aec OCA], [https://pdbe.org/5aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aec RCSB], [https://www.ebi.ac.uk/pdbsum/5aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aec ProSAT]</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>
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 19: @@
 </div>
 <div class="pdbe-citations 5aec" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Beecher, J]]
+[[Category: Large Structures]]
-[[Category: Bornscheuer, U T]]
+[[Category: Pseudomonas putida]]
-[[Category: Bourenkov, G]]
+[[Category: Beecher J]]
-[[Category: Davenport, C F]]
+[[Category: Bornscheuer UT]]
-[[Category: Dcunha, S]]
+[[Category: Bourenkov G]]
-[[Category: Donadio, G]]
+[[Category: Davenport CF]]
-[[Category: Gibson, R P]]
+[[Category: Dcunha S]]
-[[Category: Hasegawa, Y]]
+[[Category: Donadio G]]
-[[Category: Isupov, M N]]
+[[Category: Gibson RP]]
-[[Category: Iwaki, H]]
+[[Category: Hasegawa Y]]
-[[Category: Kadow, M]]
+[[Category: Isupov MN]]
-[[Category: Lau, P C]]
+[[Category: Iwaki H]]
-[[Category: Littlechild, J A]]
+[[Category: Kadow M]]
-[[Category: Loschinski, K]]
+[[Category: Lau PC]]
-[[Category: McGhie, E J]]
+[[Category: Littlechild JA]]
-[[Category: Saneei, V]]
+[[Category: Loschinski K]]
-[[Category: Sayer, C]]
+[[Category: McGhie EJ]]
-[[Category: Schroeder, E]]
+[[Category: Saneei V]]
-[[Category: Biocatalysis]]
+[[Category: Sayer C]]
-[[Category: Flavin monooxygenase]]
+[[Category: Schroeder E]]
-[[Category: Oxidoreductase]]

5aec

From Proteopedia

Current revision

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

Function

Publication Abstract from PubMed

See Also

References

Contents

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