3FLM
Crystal structure of menD from E.coli
Summary for 3FLM
| Entry DOI | 10.2210/pdb3flm/pdb |
| Descriptor | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (2 entities in total) |
| Functional Keywords | menaquinone biosynthesis protein, magnesium, manganese, menaquinone biosynthesis, metal-binding, thiamine pyrophosphate, transferase |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 2 |
| Total formula weight | 122899.66 |
| Authors | Priyadarshi, A.,Hwang, K.Y. (deposition date: 2008-12-19, release date: 2009-03-24, Last modification date: 2023-11-01) |
| Primary citation | Priyadarshi, A.,Saleem, Y.,Nam, K.H.,Kim, K.S.,Park, S.Y.,Kim, E.E.,Hwang, K.Y. Structural insights of the MenD from Escherichia coli reveal ThDP affinity. Biochem.Biophys.Res.Commun., 380:797-801, 2009 Cited by PubMed Abstract: MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate) synthase belongs to the superfamily of thiamin diphosphate-dependent decarboxylases, which converts isochorismate and 2-oxoglutarate to SHCHC, pyruvate, and carbon dioxide. Here, we report the first crystal structure of apo-MenD from Escherichia coli determined in tetragonal crystal form. The subunit displays the typical three-domain structure observed for ThDP-dependent enzymes. Analytical gel filtration shows that EcMenD behaves as a dimer as well as a tetramer. Circular dichroism and isothermal calorimetry results confirm EcMenD dependency on ThDP, which concomitantly helps to stabilize with better configuration. PubMed: 19338755DOI: 10.1016/j.bbrc.2009.01.168 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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