3BXY

Crystal structure of tetrahydrodipicolinate N-succinyltransferase from E. coli

Summary for 3BXY

• Entry DOI: 10.2210/pdb3bxy/pdb
• Related: 1kgq 1kgt 1tdt 2tdt 3tdt
• Descriptor: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (2 entities in total)
• Functional Keywords: left-handed beta-helix, structural genomics, cihr, canadian institutes of health research, montreal-kingston bacterial structural genomics initiative, bsgi, acyltransferase, amino-acid biosynthesis, diaminopimelate biosynthesis, lysine biosynthesis, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (By similarity): Q8X8Y7
• Total number of polymer chains: 1
• Total formula weight: 31114.21

Authors

Kozlov, G.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2008-01-15, release date: 2008-01-29, Last modification date: 2023-08-30)

Primary citation

Nguyen, L.,Kozlov, G.,Gehring, K.
Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding.
Febs Lett., 582:623-626, 2008

PubMed Abstract: 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 A 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.

PubMed: 18242192
DOI: 10.1016/j.febslet.2008.01.032

Experimental method

X-RAY DIFFRACTION (2 Å)