Mutagenesis Studies of Substrate Recognition and Catalysis in the Sortase A Transpeptidase from Staphylococcus aureus

• Published in: The Journal of biological chemistry Vol. 283; no. 21; pp. 14762 - 14771
• Main Authors: Bentley, Matthew L., Lamb, Erin C., McCafferty, Dewey G.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 23.05.2008; American Society for Biochemistry and Molecular Biology
• Subjects: Aminoacyltransferases - chemistry; Aminoacyltransferases - genetics; Aminoacyltransferases - metabolism; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Binding Sites; Catalysis; Crystallography, X-Ray; Cysteine Endopeptidases - chemistry; Cysteine Endopeptidases - genetics; Cysteine Endopeptidases - metabolism; Enzyme Catalysis and Regulation; Kinetics; Models, Molecular; Mutagenesis - genetics; Mutation - genetics; Peptidyl Transferases - chemistry; Peptidyl Transferases - genetics; Peptidyl Transferases - metabolism; Protein Denaturation; Protein Structure, Tertiary; Staphylococcus aureus; Staphylococcus aureus - enzymology; Staphylococcus aureus - genetics; Substrate Specificity; Temperature

The Staphylococcus aureus transpeptidase sortase A (SrtA) is responsible for anchoring a range of virulence- and colonization-associated proteins to the cell wall. SrtA recognizes substrates that contain a C-terminal LPXTG motif. This sequence is cleaved following the threonine, and an amide bond is...