In:
Acta Crystallographica Section D Structural Biology, International Union of Crystallography (IUCr), Vol. 78, No. 5 ( 2022-05-01), p. 586-598
Abstract:
Phenylalanine hydroxylase (PAH), which belongs to the aromatic amino-acid hydroxylase family, is involved in protein synthesis and pyomelanine production through the hydroxylation of phenylalanine to tyrosine. In this study, the crystal structure of PAH from Bacillus cereus ATCC 14579 ( Bc PAH) with an additional 280 amino acids in the C-terminal region was determined. The structure of Bc PAH consists of three distinct domains: a core domain with two additional inserted α-helices and two novel auxiliary domains: Bc PAH-AD1 and Bc PAH-AD2. Structural homologues of Bc PAH-AD1 and Bc PAH-AD2 are known to be involved in mRNA regulation and protein–protein interactions, and thus it was speculated that Bc PAH might utilize the auxiliary domains for interaction with its partner proteins. Furthermore, phylogenetic tree analysis revealed that the three-domain PAHs, including Bc PAH, are completely distinctive from both conventional prokaryotic PAHs and eukaryotic PAHs. Finally, biochemical studies of Bc PAH showed that Bc PAH-AD1 might be important for the structural integrity of the enzyme and that Bc PAH-AD2 is related to enzyme stability and/or activity. Investigations into the intracellular functions of the two auxiliary domains and the relationship between these functions and the activity of PAH are required.
Type of Medium:
Online Resource
ISSN:
2059-7983
DOI:
10.1107/S2059798322002674
DOI:
10.1107/S2059798322002674/ud5033sup1.pdf
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2022
detail.hit.zdb_id:
2968623-4
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