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Related Experiment Videos

Active site restructuring regulates ligand recognition in class A penicillin-binding proteins.

Pauline Macheboeuf1, Anne Marie Di Guilmi, Viviana Job

  • 1Laboratoires de Cristallographie Macromoléculaire, Centre National de la Recherche Scientifique/Commissariat à l'Energie Atomique/Université Joseph Fourier, 41 Rue Jules Horowitz, 38027 Grenoble, France.

Proceedings of the National Academy of Sciences of the United States of America
|January 8, 2005
PubMed
Summary

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The crystal structure of pneumococcal penicillin-binding protein 1b (PBP1b) reveals its three-domain structure and how it binds to beta-lactam antibiotics. This provides insights into bacterial cell division and antibiotic resistance mechanisms.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Bacterial cell division relies on peptidoglycan biosynthesis by penicillin-binding proteins (PBPs).
  • Streptococcus pneumoniae utilizes three bifunctional class A PBPs for cell wall synthesis.
  • PBPs are crucial targets for beta-lactam antibiotics and are implicated in drug resistance.

Purpose of the Study:

  • To determine the crystal structure of a soluble form of pneumococcal PBP1b (PBP1b*).
  • To elucidate the structural basis for beta-lactam antibiotic recognition by class A PBPs.
  • To provide insights into the activation mechanism of class A PBPs during cell division and antibiotic resistance.

Main Methods:

  • X-ray crystallography was used to solve the structure of PBP1b* to 1.9 Å resolution.

Related Experiment Videos

  • Structural analysis of PBP1b* in complex with beta-lactam antibiotics.

    • Main Results:

    • The solved structure reveals PBP1b* as a three-domain molecule.
    • Ligand recognition involves conformational changes within a conserved cleft.
    • Distinct open and closed conformations of PBP1b* were observed, suggesting a mechanism for activation.

    Conclusions:

    • The structure of PBP1b* offers unprecedented insights into class A PBP function.
    • Understanding PBP1b* structure is crucial for developing new antibiotics and combating resistance.
    • The findings provide a framework for studying the role of class A PBPs in antibiotic resistance.