3uox: Difference between revisions

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<StructureSection load='3uox' size='340' side='right'caption='[[3uox]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
<StructureSection load='3uox' size='340' side='right'caption='[[3uox]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3uox]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UOX FirstGlance]. <br>
<table><tr><td colspan='2'>[[3uox]] 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=3UOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UOX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 1.956&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3uov|3uov]], [[3uoy|3uoy]], [[3uoz|3uoz]], [[3up4|3up4]], [[3up5|3up5]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">otemo ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</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=3uox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uox OCA], [https://pdbe.org/3uox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uox RCSB], [https://www.ebi.ac.uk/pdbsum/3uox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uox ProSAT]</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=3uox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uox OCA], [https://pdbe.org/3uox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uox RCSB], [https://www.ebi.ac.uk/pdbsum/3uox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uox ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/OTEMO_PSEPU OTEMO_PSEPU] Involved in the degradation of (+)-camphor. Catalyzes the lactonization of 2-oxo-delta(3)-4,5, 5-trimethylcyclopentenylacetyl-CoA (OT-CoA), a key intermediate in the metabolism of camphor. 2-Oxocyclopentyl ethyl acetate is also a good substrate, as is 2-oxocyclohexyl ethyl acetate and methyl-substituted cyclohexanones, but free acid is a poor substrate.<ref>PMID:22267661</ref> <ref>PMID:22286514</ref> <ref>PMID:6848481</ref>  
A dimeric Baeyer-Villiger monooxygenase (BVMO) catalyzing the lactonization of 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-CoA, a key intermediate in the metabolism of camphor by Pseudomonas putida ATCC 17453 had been initially characterized in 1983 by Trudgill and co-workers (H.J. Ougham, D.G. Taylor, and P.W. Trudgill, J. Bacteriol. 153:140-152, 1983). Here we have cloned and overexpressed the 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase (OTEMO) in Escherichia coli, and determined its three-dimensional structure with bound FAD at 1.95 A resolution as well as with bound FAD and NADP(+) at 2.0 A resolution. OTEMO represents the first homodimeric type 1 BVMO structure bound to FAD/NADP(+). Comparison of several crystal forms of OTEMO bound to FAD and NADP(+) revealed conformational plasticity of several loop regions, some of which have been implicated as contributing to the substrate specificity profile of structurally-related BVMOs. Substrate specificity studies confirmed that the 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetic acid coenzyme A ester is preferred over the free acid. However, the catalytic efficiency (k(cat)/K(m)) favors 2-n-hexyl cyclopentanone (4.3 x 10(5) M(-1)s(-1)) as a substrate, although its affinity (K(m) = 32 muM) was lower than that of the CoA-activated substrate (18 muM). In whole cell biotransformation experiments, OTEMO showed a unique enantiocomplementarity to the action of the prototypical cyclohexanone monooxygenase (CHMO), and appeared to be particularly useful for the oxidation of 4-substituted cyclohexanones. Overall, this work expands our understanding of the molecular structure and mechanistic complexity of the type 1 family of BVMOs as well as expanding the catalytic repertoire of one of its original members.
 
Camphor Pathway 2-Oxo-{Delta}3-4,5,5-trimethylcyclopentenylacetyl-CoA Monooxygenase of Pseudomonas putida ATCC 17453: Cloning, Baeyer-Villiger Biooxidations, and Structures.,Leisch H, Shi R, Grosse S, Morley K, Bergeron H, Cygler M, Iwaki H, Hasegawa Y, Lau PC Appl Environ Microbiol. 2012 Jan 20. PMID:22267661<ref>PMID:22267661</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3uox" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus fluorescens putidus flugge 1886]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cygler, M]]
[[Category: Pseudomonas putida]]
[[Category: Lau, P]]
[[Category: Cygler M]]
[[Category: Matte, A]]
[[Category: Lau P]]
[[Category: Shi, R]]
[[Category: Matte A]]
[[Category: Baeyer-villiger monooxygenase]]
[[Category: Shi R]]
[[Category: Oxidoreductase]]

Revision as of 14:04, 14 March 2024

Crystal Structure of OTEMO (FAD bound form 2)

3uox, resolution 1.96Å

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