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Researchers used mix-and-inject serial crystallography to observe the Mycobacterium tuberculosis enzyme BlaC

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Elucidating enzyme mechanisms at atomic resolution is crucial for understanding biological processes.
  • Real-time atomic position tracing offers unprecedented insights into enzyme dynamics.
  • X-ray free electron laser (XFEL) facilities enable time-resolved crystallography.

Approach:

  • Mix-and-inject serial crystallography (MISC) was employed at an XFEL.
  • Enzymatic reactions were initiated by mixing substrates with enzyme microcrystals.
  • Singular value decomposition (SVD) was applied to analyze the crystallographic data.

Key Points:

  • Atomic-level details of sulbactam (SUB) inhibition of Mycobacterium tuberculosis BlaC were captured.
  • Ligand binding heterogeneity, gating, cooperativity, induced fit, and conformational selection were observed.
  • The study reveals the non-covalent binding of SUB to BlaC before reaction to a trans-enamine.

Conclusions:

  • MISC provides a powerful platform for time-resolved structural studies of enzyme inhibition.
  • The dynamic mechanisms of enzyme inhibition can be elucidated in atomic detail.
  • This work advances our understanding of BlaC inhibition and opens avenues for drug design.