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Isomerase PDB id
2gbb
Jmol
Contents
Protein chains
156 a.a. *
Ligands
SO4 ×13
CIT ×4
Waters ×193
* Residue conservation analysis
PDB id:
2gbb
Name: Isomerase
Title: Crystal structure of secreted chorismate mutase from yersinia pestis
Structure: Putative chorismate mutase. Chain: a, b, c, d. Engineered: yes
Source: Yersinia pestis biovar microtus str. 91001. Organism_taxid: 229193. Strain: kim. Gene: y2828. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.207     R-free:   0.258
Authors: J.E.Ladner,P.T.Reddy,B.C.Nelson,H.Robinson,S.-K.Kim
Key ref: S.K.Kim et al. (2008). A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis. Febs J, 275, 4824-4835. PubMed id: 18727669 DOI: 10.1111/j.1742-4658.2008.06621.x
Date:
10-Mar-06     Release date:   03-Apr-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

 Enzyme reactions 
   Enzyme class: E.C.5.4.99.5  - Chorismate mutase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Phenylalanine and Tyrosine Biosynthesis
      Reaction: Chorismate = prephenate
Chorismate
 =
prephenate
Bound ligand (Het Group name = CIT)
matches with 45.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1111/j.1742-4658.2008.06621.x Febs J 275:4824-4835 (2008)
PubMed id: 18727669  
 
 
A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis.
S.K.Kim, S.K.Reddy, B.C.Nelson, H.Robinson, P.T.Reddy, J.E.Ladner.
 
  ABSTRACT  
 
The Rv0948c gene from Mycobacterium tuberculosis H(37)R(v) encodes a 90 amino acid protein as the natural gene product with chorismate mutase (CM) activity. The protein, 90-MtCM, exhibits Michaelis-Menten kinetics with a k(cat) of 5.5+/-0.2s(-1) and a K(m) of 1500+/-100microm at 37 degrees C and pH7.5. The 2.0A X-ray structure shows that 90-MtCM is an all alpha-helical homodimer (Protein Data Bank ID: 2QBV) with the topology of Escherichia coli CM (EcCM), and that both protomers contribute to each catalytic site. Superimposition onto the structure of EcCM and the sequence alignment shows that the C-terminus helix3 is shortened. The absence of two residues in the active site of 90-MtCM corresponding to Ser84 and Gln88 of EcCM appears to be one reason for the low k(cat). Hence, 90-MtCM belongs to a subfamily of alpha-helical AroQ CMs termed AroQ(delta.) The CM gene (y2828) from Yersinia pestis encodes a 186 amino acid protein with an N-terminal signal peptide that directs the protein to the periplasm. The mature protein, *YpCM, exhibits Michaelis-Menten kinetics with a k(cat) of 70+/-5s(-1) and K(m) of 500+/-50microm at 37 degrees C and pH7.5. The 2.1A X-ray structure shows that *YpCM is an all alpha-helical protein, and functions as a homodimer, and that each protomer has an independent catalytic unit (Protein Data Bank ID: 2GBB). *YpCM belongs to the AroQ(gamma) class of CMs, and is similar to the secreted CM (Rv1885c, *MtCM) from M.tuberculosis.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19236568 B.Vanholme, P.Kast, A.Haegeman, J.Jacob, W.Grunewald, and G.Gheysen (2009).
Structural and functional investigation of a secreted chorismate mutase from the plant-parasitic nematode Heterodera schachtii in the context of related enzymes from diverse origins.
  Mol Plant Pathol, 10, 189-200.  
19556970 S.Sasso, M.Okvist, K.Roderer, M.Gamper, G.Codoni, U.Krengel, and P.Kast (2009).
Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner.
  EMBO J, 28, 2128-2142.
PDB codes: 2vkl 2w19 2w1a
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.