• Publications
  • Influence
Structure and functions of the GNAT superfamily of acetyltransferases.
Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis
The three-dimensional structures of wild-type and mutant InhA revealed that drug resistance is directly related to a perturbation in the hydrogen-bonding network that stabilizes NADH binding.
A Fluoroquinolone Resistance Protein from Mycobacterium tuberculosis That Mimics DNA
Its three-dimensional structure reveals a fold, which is named the right-handed quadrilateral β helix, that exhibits size, shape, and electrostatic similarity to B-form DNA and explains both its inhibitory effect on DNA gyrase and fluoroquinolone resistance resulting from the protein's expression in vivo.
Meropenem-Clavulanate Is Effective Against Extensively Drug-Resistant Mycobacterium tuberculosis
When meropenem was combined with the β-lactamase inhibitor clavulanate, potent activity against laboratory strains of M. tuberculosis was observed and could potentially be used to treat patients with currently untreatable disease.
Flavoprotein disulfide reductases: advances in chemistry and function.
Structural and Enzymatic Analysis of MshA from Corynebacterium glutamicum
Molecular models of the ternary complex suggest a mechanism in which the β-phosphate of the substrate, UDP-N-acetylglucosamine, promotes the nucleophilic attack of the 3-hydroxyl group of 1-l-myo-inositol-1- phosphate while at the same time promoting the cleavage of the sugar nucleotide bond.
Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase.
It is suggested that mycothione reductase, cloned, expressed in Mycobacterium smegmatis, and purified 145-fold to homogeneity in 43% yield, is the newest member of the class I flavoprotein disulfide reduct enzyme family of oxidoreductases.
Pentapeptide repeat proteins.
The three-dimensional structure of the first member of the PRP family was determined for the fluoroquinolone resistance protein (MfpA) from Mycobacterium tuberculosis and revealed that the pentapeptide repeats encode the folding of a novel right-handed quadrilateral beta-helix.
Structure of QnrB1, a Plasmid-mediated Fluoroquinolone Resistance Factor*
A mechanism in which PRP-topoisomerase poison resistance factors bind to and disrupt the quinolone-DNA-gyrase interaction is proposed.