3BZM
Crystal Structure of Open form of Menaquinone-Specific Isochorismate Synthase, MenF
Summary for 3BZM
| Entry DOI | 10.2210/pdb3bzm/pdb |
| Related | 3BZN |
| Descriptor | Menaquinone-specific isochorismate synthase, CITRIC ACID (3 entities in total) |
| Functional Keywords | chorismate, isochorismate, menaquinone, isomerase, menaquinone biosynthesis |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 49015.55 |
| Authors | Parsons, J.F.,Shi, K.M.,Ladner, J.E. (deposition date: 2008-01-18, release date: 2008-05-20, Last modification date: 2024-02-21) |
| Primary citation | Parsons, J.F.,Shi, K.M.,Ladner, J.E. Structure of isochorismate synthase in complex with magnesium. Acta Crystallogr.,Sect.D, 64:607-610, 2008 Cited by PubMed Abstract: The electron carrier menaquinone is one of many important bacterial metabolites that are derived from the key intermediate chorismic acid. MenF, the first enzyme in the menaquinone pathway, catalyzes the isomerization of chorismate to isochorismate. Here, an improved structure of MenF in a new crystal form is presented. The structure, solved at 2.0 angstroms resolution in complex with magnesium, reveals a well defined closed active site. Existing evidence suggests that the mechanism of the reaction catalyzed by MenF involves nucleophilic attack of a water molecule on the chorismate ring. The structure reveals a well defined water molecule located in an appropriate position for activation by Lys190 and attack on the substrate. PubMed: 18453696DOI: 10.1107/S0907444908005477 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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