9fcg

Medicago truncatula 5'-ProFAR isomerase (HISN3) D57N mutant in complex with PrFAR

spinqualitylabelsall models 9fcg, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9fcg is a 1 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 1.54Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G7IFI7_MEDTR Publication Abstract from PubMed Histidine biosynthesis is essential for the growth and development of plants, where it occurs within chloroplasts. The eleven reactions are catalyzed by eight enzymes, known as HISN1-8, each acting sequentially. Here, we present the crystal structures of a 5'-ProFAR isomerase (HISN3) from the model legume Medicago truncatula bound to its enzymatically synthesized substrate (ProFAR) and product (PrFAR). The active site of MtHISN3 contains a sodium cation that participates in ligand recognition, a feature not observed in bacterial and fungal structures of homologous enzymes. The steady-state kinetics of wild-type MtHISN3 revealed a slightly higher turnover rate compared to its bacterial homologs. Plant HISN3 sequences contain an unusually elongated Lys60-Ser91 fragment, while deletion of the 74-80 region resulted in a 30-fold loss in catalytic efficiency compared to the wild-type. Molecular dynamics simulations suggested that the fragment facilitates product release, thereby contributing to a higher k(cat). Moreover, conservation analyses suggested a non-cyanobacterial origin for plant HISN3 enzymes, which is another instance of a non-cyanobacterial enzyme in the plant histidine biosynthetic pathway. Finally, a virtual screening campaign yielded five molecules, with the energy gains ranging between -13.6 and -13.1 kcal/mol, which provide new scaffolds for the future development of herbicides. Structural, kinetic, and evolutionary peculiarities of HISN3, a plant 5'-ProFAR isomerase.,Witek W, Imiolczyk B, Ruszkowski M Plant Physiol Biochem. 2024 Aug 22;215:109065. doi: 10.1016/j.plaphy.2024.109065. PMID:39186852 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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