spacer
spacer

PDBsum entry 2eua

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Isomerase PDB id
2eua
Jmol
Contents
Protein chains
428 a.a. *
Ligands
TAR ×2
Waters ×150
* Residue conservation analysis
PDB id:
2eua
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
Resolution:
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 DOI: 10.1021/bi0608515
Date:
28-Oct-05     Release date:   05-Dec-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P38051  (MENF_ECOLI) -  Menaquinone-specific isochorismate synthase
Seq:
Struc:
431 a.a.
428 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.4.4.2  - Isochorismate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Shikimate and Chorismate Biosynthesis
      Reaction: Chorismate = isochorismate
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     3 terms  

 

 
    Added reference    
 
 
DOI no: 10.1021/bi0608515 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.
 
  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.
 

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
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.