1TDT

THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINYLTRANSFERASE

Summary for 1TDT

• Entry DOI: 10.2210/pdb1tdt/pdb
• Descriptor: TETRAHYDRODIPICOLINATE-N-SUCCINYLTRANSFERASE (2 entities in total)
• Functional Keywords: transferase, succinyltransferase, lysine metabolism, hexapeptide transferase, cell wall biosynthesis
• Biological source: Mycobacterium bovis
• Cellular location: Cytoplasm: P56220
• Total number of polymer chains: 3
• Total formula weight: 84747.17

Authors

Beaman, T.W.,Binder, D.W.,Blanchard, J.S.,Roderick, S.L. (deposition date: 1996-11-19, release date: 1997-06-05, Last modification date: 2024-02-14)

Primary citation

Beaman, T.W.,Binder, D.A.,Blanchard, J.S.,Roderick, S.L.
Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase.
Biochemistry, 36:489-494, 1997

PubMed Abstract: The conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA is catalyzed by tetrahydrodipicolinate N-succinyltransferase and is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The X-ray crystal structure of THDP succinyltransferase has been determined to 2.2 A resolution and has been refined to a crystallographic R-factor of 17.0%. The enzyme is trimeric and displays the left-handed parallel beta-helix (L beta H) structural motif encoded by the "hexapeptide repeat" amino acid sequence motif [Raetz, C.R.H., & Roderick, S.L. (1995) Science 270, 997-1000]. The approximate location of the active site of THDP succinyltransferase is suggested by the proximity of binding sites for two inhibitors: p-(chloromercuri)benzenesulfonic acid and cobalt ion, both of which bind to the L beta H domain.

PubMed: 9012664
DOI: 10.1021/bi962522q

Experimental method

X-RAY DIFFRACTION (2.2 Å)