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Isomerase PDB id
2f6l
Jmol
Contents
Protein chains
166 a.a. *
Waters ×363
* Residue conservation analysis
PDB id:
2f6l
Name: Isomerase
Title: X-ray structure of chorismate mutase from mycobacterium tube
Structure: Chorismate mutase. Chain: a, b. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Gene: rv1885c. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
1.70Å     R-factor:   0.182     R-free:   0.222
Authors: S.K.Kim,A.J.Howard,G.L.Gilliland,P.T.Reddy,J.E.Ladner
Key ref: S.K.Kim et al. (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. PubMed id: 17146044 DOI: 10.1128/JB.00441-06
Date:
29-Nov-05     Release date:   13-Dec-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O07746  (O07746_MYCTU) -  Chorismate mutase-related protein
Seq:
Struc: 		199 a.a.
166 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
 = 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: 10.1128/JB.00441-06 J Bacteriol 188:8638-8648 (2006)
PubMed id: 17146044  
 
 
Biochemical and structural characterization of the secreted chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ enzyme not regulated by the aromatic amino acids.
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, P.T.Reddy.
 
  ABSTRACT  
 
The gene Rv1885c from the genome of Mycobacterium tuberculosis H37Rv encodes a monofunctional and secreted chorismate mutase (*MtCM) with a 33-amino-acid cleavable signal sequence; hence, it belongs to the *AroQ class of chorismate mutases. Consistent with the heterologously expressed *MtCM having periplasmic destination in Escherichia coli and the absence of a discrete periplasmic compartment in M. tuberculosis, we show here that *MtCM secretes into the culture filtrate of M. tuberculosis. *MtCM functions as a homodimer and exhibits a dimeric state of the protein at a concentration as low as 5 nM. *MtCM exhibits simple Michaelis-Menten kinetics with a Km of 0.5 +/- 0.05 mM and a k(cat) of 60 s(-1) per active site (at 37 degrees C and pH 7.5). The crystal structure of *MtCM has been determined at 1.7 A resolution (Protein Data Bank identifier 2F6L). The protein has an all alpha-helical structure, and the active site is formed within a single chain without any contribution from the second chain in the dimer. Analysis of the structure shows a novel fold topology for the protein with a topologically rearranged helix containing Arg134. We provide evidence by site-directed mutagenesis that the residues Arg49, Lys60, Arg72, Thr105, Glu109, and Arg134 constitute the catalytic site; the numbering of the residues includes the signal sequence. Our investigation on the effect of phenylalanine, tyrosine, and tryptophan on *MtCM shows that *MtCM is not regulated by the aromatic amino acids. Consistent with this observation, the X-ray structure of *MtCM does not have an allosteric regulatory site.
 

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.  
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.  
19082689 S.Lim, J.R.Springstead, M.Yu, W.Bartkowski, I.Schröder, and H.G.Monbouquette (2009).
Characterization of a key trifunctional enzyme for aromatic amino acid biosynthesis in Archaeoglobus fulgidus.
  Extremophiles, 13, 191-198.  
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
17965159 C.Z.Schneider, T.Parish, L.A.Basso, and D.S.Santos (2008).
The two chorismate mutases from both Mycobacterium tuberculosis and Mycobacterium smegmatis: biochemical analysis and limited regulation of promoter activity by aromatic amino acids.
  J Bacteriol, 190, 122-134.  
18606735 M.Letek, A.A.Ocampo-Sosa, M.Sanders, U.Fogarty, T.Buckley, D.P.Leadon, P.González, M.Scortti, W.G.Meijer, J.Parkhill, S.Bentley, and J.A.Vázquez-Boland (2008).
Evolution of the Rhodococcus equi vap pathogenicity island seen through comparison of host-associated vapA and vapB virulence plasmids.
  J Bacteriol, 190, 5797-5805.  
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.