The structure of Medicago truncatula δ1-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants

Ruszkowski, Milosz; Nocek, Boguslaw; Forlani, Giuseppe; Dauter, Zbigniew

doi:10.3389/fpls.2015.00869

Title: The structure of Medicago truncatula δ¹-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants

Journal Article · Fri Oct 30 00:00:00 EDT 2015 · Frontiers in Plant Science

DOI:https://doi.org/10.3389/fpls.2015.00869· OSTI ID:1239950

Ruszkowski, Milosz ^[1]; Nocek, Boguslaw ^[2]; Forlani, Giuseppe ^[3]; Dauter, Zbigniew ^[1]

National Cancer Institute, Argonne, IL (United States)
Argonne National Lab. (ANL), Argonne, IL (United States)
Univ. of Ferrara, Ferrara (Italy)

The two pathways for proline biosynthesis in higher plants share the last step, the conversion of δ¹-pyrroline-5-carboxylate (P5C) to L-proline, which is catalyzed by P5C reductase (P5CR, EC 1.5.1.2) with the use of NAD(P)H as a coenzyme. There is increasing amount of evidence to suggest a complex regulation of P5CR activity at the post-translational level, yet the molecular basis of these mechanisms is unknown. Here we report the three-dimensional structure of the P5CR enzyme from the model legume Medicago truncatula (Mt). The crystal structures of unliganded MtP5CR decamer, and its complexes with the products NAD⁺, NADP⁺, and L-proline were refined using x-ray diffraction data (at 1.7, 1.85, 1.95, and 2.1 Å resolution, respectively). Based on the presented structural data, the coenzyme preference for NADPH over NADH was explained, and NADPH is suggested to be the only coenzyme used by MtP5CR in vivo. Moreover, the insensitivity of MtP5CR to feed-back inhibition by proline, revealed by enzymatic analysis, was correlated with structural features. Additionally, a mechanism for the modulation of enzyme activity by chloride anions is discussed, as well as the rationale for the possible development of effective enzyme inhibitors.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1239950

Journal Information:: Frontiers in Plant Science, Vol. 6; ISSN 1664-462X

Publisher:: Frontiers Research FoundationCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 35 works

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Title: The structure of Medicago truncatula δ1-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants

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Title: The structure of Medicago truncatula δ¹-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants