2EUA image
Deposition Date 2005-10-28
Release Date 2006-12-05
Last Version Date 2024-02-14
Entry Detail
PDB ID:
2EUA
Keywords:
ISOMERASE
Title:
Structure and Mechanism of MenF, the Menaquinone-Specific Isochorismate Synthase from Escherichia Coli
Biological Source:
Source Organism(s):
Escherichia coli (Taxon ID: 562)
Expression System(s):
Escherichia coli
Method Details:
Experimental Method:
X-RAY DIFFRACTION
Resolution:
2.50 Å
R-Value Free:
0.27
R-Value Work:
0.22
R-Value Observed:
0.23
Space Group:
P 43 21 2
2EUA validation report missing
Macromolecular Entities
Structures with similar UniProt ID
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:Menaquinone-specific isochori
Gene (Uniprot):menF
Chain IDs:A, B
Chain Length:431
Number of Molecules:2
Biological Source:Escherichia coli
UniProt ID:P38051 Pfam ID:PF00425 EC:5.4.4.2
Ligand Molecules
TAR
Primary Citation
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)
PMID: 17240978 DOI: 10.1021/bi0608515

Abstact

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.

Legend

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Chemical

Disease

Primary Citation of related structures
2EUJ
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