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. 2015 Aug 3;6:567. doi: 10.3389/fpls.2015.00567

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Copyright © 2015 Forlani, Makarova, Ruszkowski, Bertazzini and Nocek.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The insights into the binding of NADPH and L-Proline. (A) Three different types of interactions with the NADPH phosphate moieties can be hypothesized based on the previously characterized P5CR structures with the following residues: (Type 1) serine (S31) and arginine (R35), as observed in structure of SpP5CR (PDB id: 2AHR). (Type 2) lysine (K42) of PfP5CR (PDB id: 2RCY). (Type 3) Asparagine (N31) of NmP5CR (PDB id: 2AG8). (B) Close-up view of the motif E. Structures of enzymes with either buffer-derived molecules (phosphate ion shown in light blue and ethylene glycol molecule shown in gray) or L-proline bound (in green, as observed in the structure of SpP5CR) were superimposed. For clarity, only the structure of HsP5CR is displayed in orange.