5bsh | pdb_00005bsh

Crystal structure of Medicago truncatula (delta)1-Pyrroline-5-Carboxylate Reductase (MtP5CR) in complex with L-Proline

spinqualitylabelsall models 5bsh, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5bsh is a 10 chain structure with sequence from Medicago truncatula. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: PRO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G7KRM5_MEDTR Publication Abstract from PubMed The two pathways for proline biosynthesis in higher plants share the last step, the conversion of delta1-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 A 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. Furthermore, 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. The structure of delta-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants.,Ruszkowski M, Nocek B, Forlani G, Dauter Z Front Plant Sci. 2015 Oct 30;6:869. eCollection 2015. PMID:26579138 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pyrroline-5-carboxylate reductase

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