2ao2

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spinqualitylabelsall models 2ao2, resolution 2.070Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The 2.07 Angstrom crystal structure of Mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions

Overview

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.

About this Structure

2AO2 is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. Active as Chorismate mutase, with EC number 5.4.99.5 Full crystallographic information is available from OCA.

Reference

The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions., Qamra R, Prakash P, Aruna B, Hasnain SE, Mande SC, Biochemistry. 2006 Jun 13;45(23):6997-7005. PMID:16752890

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