PDBsum entry 2eua

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Isomerase PDB id
Protein chains
428 a.a. *
TAR ×2
Waters ×150
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Structure and mechanism of menf, the menaquinone-specific isochorismate synthase from escherichia coli
Structure: Menaquinone-specific isochorismate synthase. Chain: a, b. Synonym: isochorismate mutase. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: menf. Expressed in: escherichia coli. Expression_system_taxid: 562
2.50Å     R-factor:   0.232     R-free:   0.276
Authors: S.Kolappan,C.Kisker,J.Zwahlen,R.Zhou,P.J.Tonge
Key ref: S.Kolappan et al. (2007). 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. PubMed id: 17240978
28-Oct-05     Release date:   05-Dec-06    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P38051  (MENF_ECOLI) -  Isochorismate synthase MenF
431 a.a.
428 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Isochorismate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Shikimate and Chorismate Biosynthesis
      Reaction: Chorismate = isochorismate
Bound ligand (Het Group name = TAR)
matches with 44.00% similarity
      Cofactor: Mg(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     biosynthetic process   2 terms 
  Biochemical function     isomerase activity     4 terms  


    Added reference    
Biochemistry 46:946-953 (2007)
PubMed id: 17240978  
Lysine 190 is the catalytic base in MenF, the menaquinone-specific isochorismate synthase from Escherichia coli: implications for an enzyme family.
S.Kolappan, J.Zwahlen, R.Zhou, J.J.Truglio, P.J.Tonge, C.Kisker.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18453696 J.F.Parsons, K.M.Shi, and J.E.Ladner (2008).
Structure of isochorismate synthase in complex with magnesium.
  Acta Crystallogr D Biol Crystallogr, 64, 607-610.
PDB codes: 3bzm 3bzn
18182490 S.G.Van Lanen, S.Lin, and B.Shen (2008).
Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism.
  Proc Natl Acad Sci U S A, 105, 494-499.  
17912370 G.V.Louie, T.J.Baiga, M.E.Bowman, T.Koeduka, J.H.Taylor, S.M.Spassova, E.Pichersky, and J.P.Noel (2007).
Structure and reaction mechanism of basil eugenol synthase.
  PLoS One, 2, e993.
PDB codes: 2qw8 2qx7 2qys 2qzz 2r2g 2r6j
  18007038 V.Ulaganathan, M.F.Agacan, L.Buetow, L.B.Tulloch, and W.N.Hunter (2007).
Structure of Staphylococcus aureus1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) in complex with acetoacetyl-CoA.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 908-913.
PDB code: 2uzf
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