Insights into the substrate specificity, structure, and dynamics of plant histidinol-phosphate aminotransferase (HISN6)

Rutkiewicz, Maria; Nogues, Isabel; Witek, Wojciech; Angelaccio, Sebastiana; Contestabile, Roberto; Ruszkowski, Milosz

doi:10.1016/j.plaphy.2023.02.017

Insights into the substrate specificity, structure, and dynamics of plant histidinol-phosphate aminotransferase (HISN6)

Journal Article · Thu Feb 09 23:00:00 EST 2023 · Plant Physiology and Biochemistry

DOI:https://doi.org/10.1016/j.plaphy.2023.02.017· OSTI ID:2423486

^[1]; ^[2]; ^[1]; Angelaccio, Sebastiana ^[3]; ^[3]; ^[1]

Polish Academy of Sciences, Poznan (Poland)
Monterotondo Scalo, Rome (Italy)
Sapienza Università di Roma (Italy)

Histidinol-phosphate aminotransferase is the sixth protein (hence HISN6) in the histidine biosynthetic pathway in plants. HISN6 is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible conversion of imidazole acetol phosphate into L-histidinol phosphate (HOLP). Here, we show that plant HISN6 enzymes are closely related to the orthologs from Chloroflexota. The studied example, HISN6 from Medicago truncatula (MtHISN6), exhibits a surprisingly high affinity for HOLP, which is much higher than reported for bacterial homologs. Moreover, unlike the latter, MtHISN6 does not transaminate phenylalanine. High-resolution crystal structures of MtHISN6 in the open and closed states, as well as the complex with HOLP and the apo structure without PLP, bring new insights into the enzyme dynamics, pointing at a particular role of a string-like fragment that oscillates near the active site and participates in the HOLP binding. When MtHISN6 is compared to bacterial orthologs with known structures, significant differences arise in or near the string region. The high affinity of MtHISN6 appears linked to the particularly tight active site cavity. Finally, a virtual screening against a library of over 1.3 mln compounds revealed three sites in the MtHISN6 structure with the potential to bind small molecules. Such compounds could be developed into herbicides inhibiting plant HISN6 enzymes absent in animals, which makes them a potential target for weed control agents.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Science Centre

Grant/Contract Number:: AC02-06CH11357; W-31109-ENG-38

OSTI ID:: 2423486

Journal Information:: Plant Physiology and Biochemistry, Journal Name: Plant Physiology and Biochemistry Vol. 196; ISSN 0981-9428

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: English

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Crystal structure of Medicago truncatula histidinol-phosphate aminotransferase (HISN6) in the open state Rutkiewicz, Maria; Ruszkowski, Milosz https://doi.org/10.18150/vhekmi The current record is supplemented by this dataset	dataset	January 2023
Crystal structure of Medicago truncatula histidinol-phosphate aminotransferase (HISN6) in apo form Witek, W.; Rutkiewicz, M.; Ruszkowski, M. https://doi.org/10.18150/zeps7j The current record is supplemented by this dataset	dataset	January 2023
Crystal structure of Medicago truncatula histidinol-phosphate aminotransferase (HISN6) in complex with histidinol-phosphate Rutkiewicz, Maria; Ruszkowski, Milosz https://doi.org/10.18150/zmhott The current record is supplemented by this dataset	dataset	January 2023

Insights into the substrate specificity, structure, and dynamics of plant histidinol-phosphate aminotransferase (HISN6)

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