PDBsum entry: 2qbv

Isomerase

PDB id: 2qbv

Contents

Protein chain

73 a.a. *

Waters ×47

* Residue conservation analysis

PDB id:

2qbv

Name:

Isomerase

Title:

Crystal structure of intracellular chorismate mutase from mycobacterium tuberculosis

Structure:

Chorismate mutase. Chain: a. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Gene: rv0948c. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.00Å R-factor: 0.222 R-free: 0.298

Authors:

J.E.Ladner,P.T.Reddy,S.K.Kim,S.-K.Reddy,B.C.Nelson

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:

18-Jun-07 Release date: 26-Jun-07

Protein chain

P64767  (Y948_MYCTU) -  Uncharacterized protein Rv0948c/MT0975

Seq: 105 a.a.

Struc: 73 a.a.

Enzyme reactions

• Enzyme class: E.C.5.4.99.5 - Chorismate mutase.
• Pathway: Phenylalanine and Tyrosine Biosynthesis
• Reaction: Chorismate = prephenate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: chorismate metabolic process (1 term)

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.