Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of isochorismate synthase in complex with magnesium.,Parsons JF, Shi KM, Ladner JE Acta Crystallogr D Biol Crystallogr. 2008 May;64(Pt 5):607-10. Epub 2008, Apr 19. PMID:18453696[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Parsons JF, Shi KM, Ladner JE. Structure of isochorismate synthase in complex with magnesium. Acta Crystallogr D Biol Crystallogr. 2008 May;64(Pt 5):607-10. Epub 2008, Apr 19. PMID:18453696 doi:10.1107/S0907444908005477