Download MendeleyStructure of isochorismate synthase in complex with magnesium.
Parsons, J.F., Shi, K.M., Ladner, J.E.(2008) Acta Crystallogr D Biol Crystallogr 64: 607-610
- PubMed: 18453696
- DOI: https://doi.org/10.1107/S0907444908005477
- Primary Citation of Related Structures:
3BZM, 3BZN - 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.
Organizational Affiliation:
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, USA. [email protected]
