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Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase
Author(s) -
Girish Tavarekere S.,
Sharma Eshita,
Gopal B.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.07.035
Subject(s) - staphylococcus aureus , characterization (materials science) , microbiology and biotechnology , chemistry , biology , biochemistry , bacteria , genetics , materials science , nanotechnology
Lysine biosynthesis is crucial for cell‐wall formation in bacteria. Enzymes involved in lysine biosynthesis are thus potential targets for anti‐microbial therapeutics. Dihydrodipicolinate synthase (DHDPS) catalyzes the first step of this pathway. Unlike its homologues, Staphylococcus aureus DHDPS is a dimer both in solution and in the crystal and is not feedback inhibited by lysine. The crystal structure of S. aureus DHDPS in the free and substrate bound forms provides a structural rationale for its catalytic mechanism. The structure also reveals unique conformational features of the S. aureus enzyme that could be crucial for the design of specific non‐competitive inhibitors.