2EUA

Structure and Mechanism of MenF, the Menaquinone-Specific Isochorismate Synthase from Escherichia Coli

Summary for 2EUA

• Entry DOI: 10.2210/pdb2eua/pdb
• Related: 2EUJ
• Descriptor: Menaquinone-specific isochorismate synthase, D(-)-TARTARIC ACID (3 entities in total)
• Functional Keywords: alpha/beta fold, isomerase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 97947.02

Authors

Kolappan, S.,Kisker, C.,Zwahlen, J.,Zhou, R.,Tonge, P.J. (deposition date: 2005-10-28, release date: 2006-12-05, Last modification date: 2024-02-14)

Primary citation

Kolappan, S.,Zwahlen, J.,Zhou, R.,Truglio, J.J.,Tonge, P.J.,Kisker, C.
Lysine 190 is the catalytic base in MenF, the menaquinone-specific isochorismate synthase from Escherichia coli: implications for an enzyme family.
Biochemistry, 46:946-953, 2007

PubMed Abstract: Menaquinone biosynthesis is initiated by the conversion of chorismate to isochorismate, a reaction that is catalyzed by the menaquinone-specific isochorismate synthase, MenF. The catalytic mechanism of MenF has been probed using a combination of structural and biochemical studies, including the 2.5 A structure of the enzyme, and Lys190 has been identified as the base that activates water for nucleophilic attack at the chorismate C2 carbon. MenF is a member of a larger family of Mg2+ dependent chorismate binding enzymes catalyzing distinct chorismate transformations. The studies reported here extend the mechanism recently proposed for this enzyme family by He et al.: He, Z., Stigers Lavoie, K. D., Bartlett, P. A., and Toney, M. D. (2004) J. Am. Chem. Soc. 126, 2378-85.

PubMed: 17240978
DOI: 10.1021/bi0608515

Experimental method

X-RAY DIFFRACTION (2.5 Å)