Journal
FEBS LETTERS
Volume 582, Issue 5, Pages 623-626Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.01.032
Keywords
protein structure; succinyltransferase; THDP; DapD; lysine biosynthesis; X-ray crystallography
Funding
- NCRR NIH HHS [RR 01646] Funding Source: Medline
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Tetrahydrodipicolinate N-succinyltransferase is an enzyme present in many bacteria that catalyzes the first step of the succinylase pathway for the synthesis of meso-diaminopimelate and the amino acid L-lysine. Inhibition of the synthesis of meso-diaminopimelate, a component of peptidoglycan present in the cell wall of bacteria, is a potential route for the development of novel anti-bacterial agents. Here, we report the crystal structure of the DapD tetrahydrodipicolinate N-succinyltransferase from Escherichia coli at 2.0 angstrom resolution. Comparison of the structure with the homologous enzyme from Mycobacterium bovis reveals the C-terminal helix undergoes a large rearrangement upon substrate binding, which contributes to cooperativity in substrate binding. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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