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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Structure of the diaminopimelate epimerase DapF from Mycobacterium tuberculosis

Veeraraghavan Usha1, Lynn G Dover, David I Roper

  • 1School of Biosciences, University of Birmingham, Edgbaston, Birmingham, England.

Acta Crystallographica. Section D, Biological Crystallography
|March 25, 2009
PubMed

Insights

The crystal structure of Mycobacterium tuberculosis DapF, essential for peptidoglycan synthesis, reveals unique features. These findings offer insights into bacterial cell wall structure and potential drug targets.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Diaminopimelic acid (DAP) is crucial for bacterial peptidoglycan synthesis.
  • Mycobacterium tuberculosis peptidoglycan contains unique penicillin-resistant meso-DAP linkages.
  • DAP epimerase (DapF) is essential for interconverting DAP isomers in M. tuberculosis.

Purpose of the Study:

  • To determine the crystal structure of the ligand-free Mycobacterium tuberculosis DapF (MtDapF).
  • To understand the structural basis for DapF function in M. tuberculosis.
  • To identify potential differences compared to other bacterial DapF enzymes.

Main Methods:

  • X-ray crystallography was used to determine the 2.6 A resolution structure of MtDapF.
  • Comparative analysis with known DapF structures from other bacteria.
  • Structural modeling to predict conformational changes upon ligand binding.

Main Results:

  • The crystal structure of ligand-free MtDapF was determined, showing distinct secondary structure deviations from other DapF enzymes.
  • Modeling suggests domain movements and loop rearrangements are involved in MtDapF activation.
  • A unique tyrosine residue in MtDapF stabilizes the DAP backbone, specific to mycobacterial enzymes.

Conclusions:

  • MtDapF possesses a unique structural architecture compared to homologous enzymes.
  • Understanding these structural features is key to elucidating its catalytic mechanism.
  • The specific stabilizing tyrosine residue presents a potential target for novel antimycobacterial agents.

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