PMID:14596911

Citation	Capitani, G, Tramonti, A, Bossa, F, Grütter, MG and De Biase, D (2003) The critical structural role of a highly conserved histidine residue in group II amino acid decarboxylases. FEBS Lett. 554:41-4
Abstract	Glutamate decarboxylase is a pyridoxal 5'-phosphate (PLP)-dependent enzyme, belonging to the subset of PLP-dependent decarboxylases classified as group II. Site-directed mutagenesis of Escherichia coli glutamate decarboxylase, combined with analysis of the crystal structure, shows that a histidine residue buried in the protein core is critical for correct folding. This histidine is strictly conserved in the PF00282 PFAM family, which includes the group II decarboxylases. A similar role is proposed for residue Ser269, also highly conserved in this group of enzymes, as it provides one of the interactions stabilising His241.
Links	PubMed
Keywords	Amino Acid Sequence; Amino Acid Substitution; Conserved Sequence; Escherichia coli Proteins/chemistry; Glutamate Decarboxylase/chemistry; Glutamate Decarboxylase/genetics; Histidine; Molecular Structure; Mutagenesis, Site-Directed; Protein Conformation; Serine
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