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Isomerase PDB id
2ao2
Jmol
Contents
Protein chains
165 a.a. *
Ligands
SO4 ×5
TRP ×2
Waters ×218
* Residue conservation analysis
PDB id:
2ao2
Name: Isomerase
Title: The 2.07 angstrom crystal structure of mycobacterium tubercu chorismate mutase reveals unexpected gene duplication and s role in host-pathogen interactions
Structure: Chorismate mutase. Chain: a, b, c. Fragment: residues 35-199. Synonym: hypothetical protein rv1885c. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Gene: rv1885c. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
Resolution:
2.07Å     R-factor:   0.180     R-free:   0.224
Authors: R.Qamra,P.Prakash,B.Aruna,S.E.Hasnain,S.C.Mande,Tb Structura Genomics Consortium (Tbsgc)
Key ref: R.Qamra et al. (2006). The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions. Biochemistry, 45, 6997-7005. PubMed id: 16752890 DOI: 10.1021/bi0606445
Date:
12-Aug-05     Release date:   13-Jun-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O07746  (O07746_MYCTU) -  Chorismate mutase-related protein
Seq:
Struc: 		199 a.a.
165 a.a.
Key:    PfamA domain  Secondary structure

 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
Bound ligand (Het Group name = TRP)
matches with 40.00% similarity 		= prephenate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     chorismate metabolic process   1 term 

 

 
    Added reference    
 
 
DOI no: 10.1021/bi0606445 Biochemistry 45:6997-7005 (2006)
PubMed id: 16752890  
 
 
The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions.
R.Qamra, P.Prakash, B.Aruna, S.E.Hasnain, S.C.Mande.
 
  ABSTRACT  
 
Chorismate mutase catalyzes the first committed step toward the biosynthesis of the aromatic amino acids, phenylalanine and tyrosine. While this biosynthetic pathway exists exclusively in the cell cytoplasm, the Mycobacterium tuberculosis enzyme has been shown to be secreted into the extracellular medium. The secretory nature of the enzyme and its existence in M. tuberculosis as a duplicated gene are suggestive of its role in host-pathogen interactions. We report here the crystal structure of homodimeric chorismate mutase (Rv1885c) from M. tuberculosis determined at 2.15 A resolution. The structure suggests possible gene duplication within each subunit of the dimer (residues 35-119 and 130-199) and reveals an interesting proline-rich region on the protein surface (residues 119-130), which might act as a recognition site for protein-protein interactions. The structure also offers an explanation for its regulation by small ligands, such as tryptophan, a feature previously unknown in the prototypical Escherichia coli chorismate mutase. The tryptophan ligand is found to be sandwiched between the two monomers in a dimer contacting residues 66-68. The active site in the "gene-duplicated" monomer is occupied by a sulfate ion and is located in the first half of the polypeptide, unlike in the Saccharomyces cerevisiae (yeast) enzyme, where it is located in the later half. We hypothesize that the M. tuberculosis chorismate mutase might have a role to play in host-pathogen interactions, making it an important target for designing inhibitor molecules against the deadly pathogen.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20176569 N.Sharadamma, Y.Harshavardhana, P.Singh, and K.Muniyappa (2010).
Mycobacterium tuberculosis nucleoid-associated DNA-binding protein H-NS binds with high-affinity to the Holliday junction and inhibits strand exchange promoted by RecA protein.
  Nucleic Acids Res, 38, 3555-3569.  
19296440 B.Taneja, J.Yadav, T.K.Chakraborty, and S.K.Brahmachari (2009).
An Indian effort towards affordable drugs: "generic to designer drugs".
  Biotechnol J, 4, 348-360.  
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.  
19589834 P.P.Li, Y.J.Liu, and S.J.Liu (2009).
Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum.
  Microbiology, 155, 3382-3391.  
17428787 S.Lun, and W.R.Bishai (2007).
Characterization of a novel cell wall-anchored protein with carboxylesterase activity required for virulence in Mycobacterium tuberculosis.
  J Biol Chem, 282, 18348-18356.  
17146044 S.K.Kim, S.K.Reddy, B.C.Nelson, G.B.Vasquez, A.Davis, A.J.Howard, S.Patterson, G.L.Gilliland, J.E.Ladner, and P.T.Reddy (2006).
Biochemical and structural characterization of the secreted chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ enzyme not regulated by the aromatic amino acids.
  J Bacteriol, 188, 8638-8648.
PDB code: 2f6l
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