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Structure of Escherichia coli tetrahydrodipicolinate N ‐succinyltransferase reveals the role of a conserved C‐terminal helix in cooperative substrate binding
Author(s) -
Nguyen Long,
Kozlov Guennadi,
Gehring Kalle
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.2008.01.032
Subject(s) - peptidoglycan , escherichia coli , cooperativity , biochemistry , bacterial cell structure , substrate (aquarium) , transferase , binding site , bacteria , lysine , helix (gastropod) , chemistry , enzyme , stereochemistry , hydrolase , biology , amino acid , ecology , genetics , snail , gene
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 Å 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.