3ucl: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==Cyclohexanone-bound crystal structure of cyclohexanone monooxygenase in the Rotated conformation== | ||
<StructureSection load='3ucl' size='340' side='right' caption='[[3ucl]], [[Resolution|resolution]] 2.36Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ucl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_sp._hi-31 Rhodococcus sp. hi-31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UCL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UCL FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYH:CYCLOHEXANONE'>CYH</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gwf|3gwf]], [[3gwd|3gwd]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chnB, chnB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=638919 Rhodococcus sp. HI-31])</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclohexanone_monooxygenase Cyclohexanone monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.22 1.14.13.22] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ucl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ucl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ucl RCSB], [http://www.ebi.ac.uk/pdbsum/3ucl PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Baeyer-Villiger monooxygenases (BVMOs) are a family of bacterial flavoproteins that catalyze the synthetically useful Baeyer-Villiger oxidation reaction. This involves the conversion of ketones into esters or cyclic ketones into lactones by introducing an oxygen atom adjacent to the carbonyl group. The BVMOs offer exquisite regio- and enantiospecificity while acting on a wide range of substrates. They use only NADPH and oxygen as co-substrates, and produce only NADP<sup>+</sup> and water as by-products, making them environmentally attractive for industrial purposes. Here, we report the first crystal structure of a BVMO, cyclohexanone monooxygenase (CHMO) from <italic>Rhodococcus</italic> sp. HI-31 in complex with its substrate, cyclohexanone, as well as NADP<sup>+</sup> and FAD, to 2.4 A resolution. This structure shows a drastic rotation of the NADP<sup>+</sup> cofactor in comparison to previously reported NADP<sup>+</sup>-bound structures, as the nicotinamide moiety is no longer positioned above the flavin ring. Instead, the substrate, cyclohexanone, is found at this location, in an appropriate position for the formation of the Criegee intermediate. The rotation of NADP<sup>+</sup> permits the substrate to gain access to the reactive flavin peroxyanion intermediate while preventing it from diffusing out of the active site. The structure thus reveals the conformation of the enzyme during the key catalytic step. CHMO is proposed to undergo a series of conformational changes to gradually move the substrate from the solvent, via binding in a solvent excluded pocket that dictates the enzyme's chemospecificity, to a location above the flavin-peroxide adduct where catalysis occurs. | |||
The substrate-bound crystal structure of a Baeyer-Villiger monooxygenase exhibits a Criegee-like conformation.,Yachnin BJ, Sprules T, McEvoy MB, Lau PC, Berghuis AM J Am Chem Soc. 2012 Apr 16. PMID:22506764<ref>PMID:22506764</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Cyclohexanone monooxygenase]] | [[Category: Cyclohexanone monooxygenase]] | ||
[[Category: Rhodococcus sp. hi-31]] | |||
[[Category: Berghuis, A M.]] | [[Category: Berghuis, A M.]] | ||
[[Category: Yachnin, B J.]] | [[Category: Yachnin, B J.]] | ||
Revision as of 08:53, 5 June 2014
Cyclohexanone-bound crystal structure of cyclohexanone monooxygenase in the Rotated conformationCyclohexanone-bound crystal structure of cyclohexanone monooxygenase in the Rotated conformation
Structural highlights
Publication Abstract from PubMedThe Baeyer-Villiger monooxygenases (BVMOs) are a family of bacterial flavoproteins that catalyze the synthetically useful Baeyer-Villiger oxidation reaction. This involves the conversion of ketones into esters or cyclic ketones into lactones by introducing an oxygen atom adjacent to the carbonyl group. The BVMOs offer exquisite regio- and enantiospecificity while acting on a wide range of substrates. They use only NADPH and oxygen as co-substrates, and produce only NADP<sup>+</sup> and water as by-products, making them environmentally attractive for industrial purposes. Here, we report the first crystal structure of a BVMO, cyclohexanone monooxygenase (CHMO) from <italic>Rhodococcus</italic> sp. HI-31 in complex with its substrate, cyclohexanone, as well as NADP<sup>+</sup> and FAD, to 2.4 A resolution. This structure shows a drastic rotation of the NADP<sup>+</sup> cofactor in comparison to previously reported NADP<sup>+</sup>-bound structures, as the nicotinamide moiety is no longer positioned above the flavin ring. Instead, the substrate, cyclohexanone, is found at this location, in an appropriate position for the formation of the Criegee intermediate. The rotation of NADP<sup>+</sup> permits the substrate to gain access to the reactive flavin peroxyanion intermediate while preventing it from diffusing out of the active site. The structure thus reveals the conformation of the enzyme during the key catalytic step. CHMO is proposed to undergo a series of conformational changes to gradually move the substrate from the solvent, via binding in a solvent excluded pocket that dictates the enzyme's chemospecificity, to a location above the flavin-peroxide adduct where catalysis occurs. The substrate-bound crystal structure of a Baeyer-Villiger monooxygenase exhibits a Criegee-like conformation.,Yachnin BJ, Sprules T, McEvoy MB, Lau PC, Berghuis AM J Am Chem Soc. 2012 Apr 16. PMID:22506764[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||||