1xf8 | pdb_00001xf8
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Crystal Structure of Weissella viridescens FemX (Y254F) Mutant
Overview
Weissella viridescens FemX (FemX(Wv)) belongs to the Fem family of, nonribosomal peptidyl transferases that use aminoacyl-tRNA as the amino, acid donor to synthesize the peptide cross-bridge found in the, peptidoglycan of many species of pathogenic gram-positive bacteria. We, have recently solved the crystal structure of FemX(Wv) in complex with the, peptidoglycan precursor UDP-MurNAc-pentapeptide and report here the, site-directed mutagenesis of nine residues located in the binding cavity, for this substrate. Two substitutions, Lys36Met and Arg211Met, depressed, FemX(Wv) transferase activity below detectable levels without affecting, protein folding. Analogues of UDP-MurNAc-pentapeptide lacking the, phosphate groups or the C-terminal D-alanyl residues were not substrates, of the enzyme. These results indicate that Lys36 and Arg211 participate in, a complex hydrogen bond network that connects the C-terminal D-Ala, residues to the phosphate groups of UDP-MurNAc-pentapeptide and constrains, the substrate in a conformation that is essential for transferase, activity.
About this Structure
1XF8 is a Single protein structure of sequence from Weissella viridescens with MG as ligand. Active as UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase, with EC number 2.3.2.10 Full crystallographic information is available from OCA.
Reference
Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens., Maillard AP, Biarrotte-Sorin S, Villet R, Mesnage S, Bouhss A, Sougakoff W, Mayer C, Arthur M, J Bacteriol. 2005 Jun;187(11):3833-8. PMID:15901708
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