Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features. - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Structure / Struct Fold Des; Structure (Camb ) Année : 2007

Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features.

Résumé

We report the structure of a strictly mitochondrial human synthetase, namely tyrosyl-tRNA synthetase (mt-TyrRS), in complex with an adenylate analog at 2.2 A resolution. The structure is that of an active enzyme deprived of the C-terminal S4-like domain and resembles eubacterial TyrRSs with a canonical tyrosine-binding pocket and adenylate-binding residues typical of class I synthetases. Two bulges at the enzyme surface, not seen in eubacterial TyrRSs, correspond to conserved sequences in mt-TyrRSs. The synthetase electrostatic surface potential differs from that of other TyrRSs, including the human cytoplasmic homolog and the mitochondrial one from Neurospora crassa. The homodimeric human mt-TyrRS shows an asymmetry propagating from the dimer interface toward the two catalytic sites and extremities of each subunit. Mutagenesis of the catalytic domain reveals functional importance of Ser200 in line with an involvement of A73 rather than N1-N72 in tyrosine identity.

Dates et versions

hal-00199322 , version 1 (18-12-2007)

Identifiants

Citer

Luc Bonnefond, Magali Frugier, Elodie Touzé, Bernard Lorber, Catherine Florentz, et al.. Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features.. Structure / Struct Fold Des; Structure (Camb ), 2007, 15 (11), pp.1505-16. ⟨10.1016/j.str.2007.09.018⟩. ⟨hal-00199322⟩

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