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. Author manuscript; available in PMC: 2015 Dec 9.
Published in final edited form as: ACS Catal. 2014 Dec 9;5(2):892–899. doi: 10.1021/cs501702k

Figure 4.

Figure 4

Conformational changes at positions 116, 296, and 375 upon substrate binding in native OYE1 and OYE variants. Ligands are highlighted in orange A.) Overlay of OYE1 (blue, PDB: 1OYA) and OYE1 with bound HBA (gray, PDB: 1K03) shows the reorientation of F296 (90° rotation of phenyl ring) and Y375 (side chain rotation). B.) OYE1(W116L) with bound (R)-carvone (PDB: 4GWE) as model for carvone binding in normal orientation. C.) OYE1(W116I) with bound (S)-carvone (PDB: 4GE8) shows substrate in flipped orientation. The re-positioning of the isopropenyl group near I116 eliminates the need for conformational changes of F296 and Y375. D.) Overlay of cpOYE303 holoenzyme (PDB: 4RNU) and cpOYE303 with bound HBA (PDB: 4RNV). Hydrogen bonding interactions and distances (in angstrom) are indicated.