The PASTA domain: a beta-lactam-binding domain

Trends Biochem Sci. 2002 Sep;27(9):438. doi: 10.1016/s0968-0004(02)02164-3.

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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / metabolism
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins*
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Databases, Protein
  • Hexosyltransferases*
  • Molecular Sequence Data
  • Muramoylpentapeptide Carboxypeptidase / chemistry
  • Muramoylpentapeptide Carboxypeptidase / genetics
  • Muramoylpentapeptide Carboxypeptidase / metabolism*
  • Penicillin-Binding Proteins
  • Peptidyl Transferases*
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases / chemistry
  • Protein-Serine-Threonine Kinases / genetics
  • Protein-Serine-Threonine Kinases / metabolism*
  • Sequence Alignment
  • beta-Lactams

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Carrier Proteins
  • Penicillin-Binding Proteins
  • beta-Lactams
  • Peptidyl Transferases
  • Hexosyltransferases
  • Protein-Serine-Threonine Kinases
  • Muramoylpentapeptide Carboxypeptidase