Abstract
Do Sequence Repeats Play an Equivalent Role in the Choline-binding Module of Pneumococcal LytA Amidase?
Highlights
The Gram-positive bacterium Streptococcus pneumoniae is an important cause of invasive disease in human population throughout the world
The LytA amidase is one of the best known bacterial autolysin that catalyzes the cleavage of the N-acetylmuramoylL-alanine bond in the peptidoglycan backbone of pneumococcus and requires the presence of choline residues in the cell wall teichoic acids for activity [4]
Genetic approaches have demonstrated that LytA amidase has evolved from the fusion of two independent modules: the NH2-terminal module, responsible for the catalytic activity, and the COOH-terminal module, involved in the recognition and attachment to the cell wall [5, 6]
Summary
The Gram-positive bacterium Streptococcus pneumoniae (pneumococcus) is an important cause of invasive disease in human population throughout the world. Genetic approaches have demonstrated that LytA amidase has evolved from the fusion of two independent modules: the NH2-terminal module, responsible for the catalytic activity, and the COOH-terminal module, involved in the recognition and attachment to the cell wall [5, 6] The latter, constructed by six repeated units (p1–p6) of 20 or 21 residues and a short COOH-terminal tail, can be expressed as an isolated protein, C-LytA, and binds the choline residues contained in the teichoic and lipoteichoic acids of the pneumococcal envelope [6]. This type of repeat is present, in varying number and position, in the murein hydrolases of pneumococcus and its bacteriophages [7,8,9]. The abbreviations used are: C-LytA, COOH-terminal module of LytA; FTIR, Fourier transform infrared spectroscopy; DSC, differential scanning calorimetry
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