Abstract
The PASTA domain (for penicillin-binding protein and serine/threonine kinase associated domain) is found in the high molecular weight penicillin-binding proteins and eukaryotic-like serine/threonine kinases of a range of pathogens. We describe this previously uncharacterized domain and infer that it binds beta-lactam antibiotics and their peptidoglycan analogues. We postulate that PknB-like kinases are key regulators of cell-wall biosynthesis. The essential function of these enzymes suggests an additional pathway for the action of beta-lactam antibiotics.
MeSH terms
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Amino Acid Sequence
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Anti-Bacterial Agents / metabolism
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Anti-Bacterial Agents / pharmacology
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Bacterial Proteins*
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Databases, Protein
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Hexosyltransferases*
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Molecular Sequence Data
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Muramoylpentapeptide Carboxypeptidase / chemistry
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Muramoylpentapeptide Carboxypeptidase / genetics
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Muramoylpentapeptide Carboxypeptidase / metabolism*
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Penicillin-Binding Proteins
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Peptidyl Transferases*
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Protein Binding
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Protein Serine-Threonine Kinases / chemistry
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism*
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Protein Structure, Tertiary
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Sequence Alignment
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beta-Lactams
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Carrier Proteins
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Penicillin-Binding Proteins
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beta-Lactams
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Peptidyl Transferases
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Hexosyltransferases
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Protein Serine-Threonine Kinases
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Muramoylpentapeptide Carboxypeptidase