structural and functional characterization of staphylococcus aureus dihydrodipicolinate synthase论文.pdf

FEBS Letters 582 (2008) 2923–2930
Structural and functional characterization of Staphylococcus aureus
dihydrodipicolinate synthase
Tavarekere S. Girish, Eshita Sharma, B. Gopal*
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
Received 20 June 2008; revised 16 July 2008; accepted 18 July 2008
Available online 29 July 2008
Edited by Hans Eklund
was resistant to front-line antibiotics. This transformation in-
Abstract Lysine biosynthesis is crucial for cell-wall formation
in bacteria. Enzymes involved in lysine biosynthesis are thus po- volved only 35 point mutations in 13 loci most of which were
tential targets for anti-microbial therapeutics. Dihydrodipicoli- localized to the purported targets of the anti-microbial agents
nate synthase (DHDPS) catalyzes the first step of this currently employed [2]. It is therefore imperative to explore
pathway. Unlike its homologues, Staphylococcus aureus DHDPS alternative targets for the design of anti-microbials in addition
is a dimer both in solution and in