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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.==
==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 ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5aec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. 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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aec ProSAT]</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>
</table>
== Function ==
== 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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5aec" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5aec" style="background-color:#fffaf0;"></div>
==See Also==
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus fluorescens putidus flugge 1886]]
[[Category: Large Structures]]
[[Category: Beecher, J]]
[[Category: Pseudomonas putida]]
[[Category: Bornscheuer, U T]]
[[Category: Beecher J]]
[[Category: Bourenkov, G]]
[[Category: Bornscheuer UT]]
[[Category: Davenport, C F]]
[[Category: Bourenkov G]]
[[Category: Dcunha, S]]
[[Category: Davenport CF]]
[[Category: Donadio, G]]
[[Category: Dcunha S]]
[[Category: Gibson, R P]]
[[Category: Donadio G]]
[[Category: Hasegawa, Y]]
[[Category: Gibson RP]]
[[Category: Isupov, M N]]
[[Category: Hasegawa Y]]
[[Category: Iwaki, H]]
[[Category: Isupov MN]]
[[Category: Kadow, M]]
[[Category: Iwaki H]]
[[Category: Lau, P C]]
[[Category: Kadow M]]
[[Category: Littlechild, J A]]
[[Category: Lau PC]]
[[Category: Loschinski, K]]
[[Category: Littlechild JA]]
[[Category: McGhie, E J]]
[[Category: Loschinski K]]
[[Category: Saneei, V]]
[[Category: McGhie EJ]]
[[Category: Sayer, C]]
[[Category: Saneei V]]
[[Category: Schroeder, E]]
[[Category: Sayer C]]
[[Category: Biocatalysis]]
[[Category: Schroeder E]]
[[Category: Flavin monooxygenase]]
[[Category: Oxidoreductase]]