0.95 Cd2+ per enzyme subunit, competes with and replaces Zn2+, binding affects the enzyme structure, three Cd2+ are coordinated by residues Asp85 and Cys86 from one monomer and Cys109 from the other monomer, the fourth Cd2+ is bound by His16 and Asp89
metalloprotein. The Zn2+ coordination site involves the three conserved cysteine residues. The C93 reactivity is modulated by the presence of the Zn2+ and Mg2+ and substantiates the role of this residue as a metal ligand
compromises the Zn2+ binding properties of the protein inducing loss of up to 90% of the metal. The enzyme is protected from inactivation by inclusion of the substrate N1-(5'-phosphoribosyl)adenosine 5'-monophosphate, while Mg2+, a metal required for catalytic activity, enhanced the rate of inactivation
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purified untagged recombinant enzyme, hanging drop vapour diffusion method, 2 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is mixed in a 1:1 ratio with reservoir solution containing 100 mM HEPES-HCl, pH 7.5, 50 mM CdSO4, 1.6 M sodium acetate, and 10% w/v glycerol, X-ray diffraction structure determination and analysis at 1.7 A resolution
Isolation and characterization of a histidine biosynthetic gene in Arabidopsis encoding a polypeptide with two separate domains for phosphoribosyl-ATP pyrophosphohydrolase and phosphoribosyl-AMP cyclohydrolase