PMID:10986463

Citation	Albert, A, Martínez-Ripoll, M, Espinosa-Ruiz, A, Yenush, L, Culiáñez-Macià, FA and Serrano, R (2000) The X-ray structure of the FMN-binding protein AtHal3 provides the structural basis for the activity of a regulatory subunit involved in signal transduction. Structure 8:961-9
Abstract	The Arabidopsis thaliana HAL3 gene product encodes for an FMN-binding protein (AtHal3) that is related to plant growth and salt and osmotic tolerance. AtHal3 shows sequence homology to ScHal3, a regulatory subunit of the Saccharomyces cerevisae serine/threonine phosphatase PPz1. It has been proposed that AtHal3 and ScHal3 have similar roles in cellular physiology, as Arabidopsis transgenic plants that overexpress AtHal3 and yeast cells that overexpress ScHal3 display similar phenotypes of improved salt tolerance. The enzymatic activity of AtHal3 has not been investigated. However, the AtHal3 sequence is homologous to that of EpiD, a flavoprotein from Staphylococcus epidermidis that recognizes a peptidic substrate and subsequently catalyzes the alpha, beta-dehydrogenation of its C-terminal cysteine residue.
Links	PubMed
Keywords	Amino Acid Sequence; Arabidopsis/genetics; Arabidopsis/physiology; Arabidopsis Proteins; Crystallography, X-Ray; Flavin Mononucleotide/metabolism; Fungal Proteins/chemistry; Models, Molecular; Molecular Sequence Data; Phosphoprotein Phosphatases/chemistry; Plant Proteins/chemistry; Plant Proteins/genetics; Plant Proteins/metabolism; Protein Structure, Secondary; Protein Subunits; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Signal Transduction
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