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240827s2024 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2024.109065
|2 doi
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|a pubmed24n1536.xml
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|a (DE-627)NLM376740493
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|a (NLM)39186852
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|a (PII)S0981-9428(24)00733-2
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|a DE-627
|b ger
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|a eng
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|a Witek, Wojciech
|e verfasserin
|4 aut
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|a Structural, kinetic, and evolutionary peculiarities of HISN3, a plant 5'-ProFAR isomerase
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|c 2024
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|a Text
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 14.09.2024
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|a Date Revised 17.09.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2024 The Authors. Published by Elsevier Masson SAS.. All rights reserved.
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|a 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 kcat. 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
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|a Journal Article
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|a (βα)(8)-barrel
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|a Herbicide resistance
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|a Histidine biosynthesis
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|a PriA
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|a TIM barrel
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|a TrpF
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|a Plant Proteins
|2 NLM
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|a Isomerases
|2 NLM
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|a EC 5.-
|2 NLM
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|a Histidine
|2 NLM
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| 650 |
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|a 4QD397987E
|2 NLM
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| 700 |
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|a Imiolczyk, Barbara
|e verfasserin
|4 aut
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| 700 |
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|a Ruszkowski, Milosz
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 215(2024) vom: 15. Sept., Seite 109065
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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|g volume:215
|g year:2024
|g day:15
|g month:09
|g pages:109065
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|u http://dx.doi.org/10.1016/j.plaphy.2024.109065
|3 Volltext
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