3DU0
E. coli dihydrodipicolinate synthase with first substrate, pyruvate, bound in active site
Summary for 3DU0
| Entry DOI | 10.2210/pdb3du0/pdb |
| Related | 1YXC |
| Descriptor | Dihydrodipicolinate synthase, POTASSIUM ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | alpha/beta barrel, tim barrel, lyase, amino-acid biosynthesis, diaminopimelate biosynthesis, lysine biosynthesis, schiff base |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 63322.44 |
| Authors | Dobson, R.C.J.,Devenish, S.R.A.,Gerrard, J.A.,Jameson, G.B. (deposition date: 2008-07-16, release date: 2008-11-18, Last modification date: 2025-03-26) |
| Primary citation | Devenish, S.R.,Gerrard, J.A.,Jameson, G.B.,Dobson, R.C. The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate. Acta Crystallogr.,Sect.F, 64:1092-1095, 2008 Cited by PubMed Abstract: Dihydrodipicolinate synthase (DHDPS) mediates the key first reaction common to the biosynthesis of (S)-lysine and meso-diaminopimelate, molecules which play a crucial cross-linking role in bacterial cell walls. An effective inhibitor of DHDPS would represent a useful antibacterial agent; despite extensive effort, a suitable inhibitor has yet to be found. In an attempt to examine the specificity of the active site of DHDPS, the enzyme was cocrystallized with the substrate analogue oxaloacetate. The resulting crystals diffracted to 2.0 A resolution, but solution of the protein structure revealed that pyruvate was bound in the active site rather than oxaloacetic acid. Kinetic analysis confirmed that the decarboxylation of oxaloacetate was not catalysed by DHDPS and was instead a slow spontaneous chemical process. PubMed: 19052357DOI: 10.1107/S1744309108033654 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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