View source for 4rg3


==Epsilon-caprolactone-bound crystal structure of cyclohexanone monooxygenase in the Tight conformation==
<StructureSection load='4rg3' size='340' side='right'caption='[[4rg3]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rg3]] is a 1 chain structure with sequence from [https://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=4RG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RG3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=ECE:CAPROLACTONE'>ECE</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=4rg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rg3 OCA], [https://pdbe.org/4rg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rg3 RCSB], [https://www.ebi.ac.uk/pdbsum/4rg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rg3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C0STX7_9NOCA C0STX7_9NOCA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Baeyer-Villiger monooxygenases (BVMOs) are microbial enzymes that catalyze the synthetically useful Baeyer-Villiger oxidation reaction. The available BVMO crystal structures all lack a substrate or product bound in a position that would determine the substrate specificity and stereospecificity of the enzyme. Here, we report two crystal structures of cyclohexanone monooxygenase (CHMO) with its product, epsilon-caprolactone, bound: the CHMOTight and CHMOLoose structures. The CHMOTight structure represents the enzyme state in which substrate acceptance and stereospecificity is determined, providing a foundation for engineering BVMOs with altered substrate spectra and/or stereospecificity. The CHMOLoose structure is the first structure where the product is solvent accessible. This structure represents the enzyme state upon binding and release of the substrate and product. In addition, the role of the invariant Arg329 in chaperoning the substrate/product during the catalytic cycle is highlighted. Overall, these data provide a structural framework for the engineering of BVMOs with altered substrate spectra and/or stereospecificity.

Lactone-bound structures of cyclohexanone monooxygenase provide insight into the stereochemistry of catalysis.,Yachnin BJ, McEvoy MB, MacCuish RJ, Morley KL, Lau PC, Berghuis AM ACS Chem Biol. 2014 Sep 29. PMID:25265531<ref>PMID:25265531</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4rg3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodococcus sp. HI-31]]
[[Category: Berghuis AM]]
[[Category: Yachnin BJ]]