3DI1
Crystal structure of the Staphylococcus aureus Dihydrodipicolinate synthase-pyruvate complex
Summary for 3DI1
| Entry DOI | 10.2210/pdb3di1/pdb |
| Related | 3DI0 |
| Descriptor | Dihydrodipicolinate synthase, PYRUVIC ACID (3 entities in total) |
| Functional Keywords | dihydrodipicolinate synthase, lysine biosynthesis, feedback inhibition, ping-pong mechanism, amino-acid biosynthesis, diaminopimelate biosynthesis, lyase, schiff base |
| Biological source | Staphylococcus aureus subsp. aureus |
| Cellular location | Cytoplasm (By similarity): Q5HG25 |
| Total number of polymer chains | 2 |
| Total formula weight | 65403.71 |
| Authors | Tavarekere, G.S. (deposition date: 2008-06-19, release date: 2008-08-12, Last modification date: 2024-10-30) |
| Primary citation | Girish, T.S.,Sharma, E.,Gopal, B. Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase Febs Lett., 582:2923-2930, 2008 Cited by PubMed Abstract: Lysine biosynthesis is crucial for cell-wall formation in bacteria. Enzymes involved in lysine biosynthesis are thus potential targets for anti-microbial therapeutics. Dihydrodipicolinate synthase (DHDPS) catalyzes the first step of this pathway. Unlike its homologues, Staphylococcus aureus DHDPS is a dimer both in solution and in the crystal and is not feedback inhibited by lysine. The crystal structure of S. aureus DHDPS in the free and substrate bound forms provides a structural rationale for its catalytic mechanism. The structure also reveals unique conformational features of the S. aureus enzyme that could be crucial for the design of specific non-competitive inhibitors. PubMed: 18671976DOI: 10.1016/j.febslet.2008.07.035 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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