Oct 20, 2007

Mutational analysis and homology modelling of SyrC, the aminoacyltransferase in the biosynthesis of syringomycin

Biochemical and Biophysical Research Communications
Maria Rosaria FulloneI Grgurina

Abstract

SyrC, a component of the multienzyme system of syringomycin biosynthesis, has been shown to shuttle Thr/4-Cl-Thr between the thiolation domains SyrB1-T1 and SyrE-T8,9 by transiently linking it to Cys224 in the enzyme active site. We present data on the structure-function relationship in vivo of this protein and an in silico model of its three-dimensional structure. The biosynthetic activity of SyrC was not influenced when either Asp348 or His376 that together with Cys224 form a putative catalytic triad, were replaced with Ala, but it was abolished by the exchange Cys224 with Ser. The presence of the FLAG peptide on either the N- or C-terminus of the protein did not affect activity, whereas the deletion of the first 16 amino acids at the N-terminus or the insertion of Maltose Binding Protein abolished the production of syringomycin. We present the model of the three-dimensional structure of SyrC suggesting a homodimeric structure for the protein and biochemical data that are supportive of this model.

Mentioned in this Paper

Syringomycin
Transverse Tubule of Muscle Cell
Poly(3-hydroxyalkanoic acid) synthase
Bacterial Proteins
TFPI gene
Chimeric Proteins, Recombinant
Enzymes, antithrombotic
Antibiotic throat preparations
Structure-Activity Relationship
Western Blotting

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