PDBsum entry: 2vkl

Isomerase

PDB id: 2vkl

Contents

Protein chain

77 a.a. *

Ligands

MLT

Waters ×37

* Residue conservation analysis

PDB id:

2vkl

Name:

Isomerase

Title:

X-ray crystal structure of the intracellular chorismate mutase from mycobactrerium tuberculosis in complex with malate

Structure:

Rv0948c/mt0975. Chain: a. Fragment: residues 16-105. Synonym: chorismate mutase. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.65Å R-factor: 0.183 R-free: 0.235

Authors:

M.Okvist,K.Roderer,S.Sasso,P.Kast,U.Krengel

Key ref:

S.Sasso et al. (2009). Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner. Embo J, 28, 2128-2142. PubMed id: 19556970 DOI: 10.1038/emboj.2009.165

Date:

20-Dec-07 Release date: 15-Jan-08

Protein chain

P64767  (Y948_MYCTU) -  Uncharacterized protein Rv0948c/MT0975

Seq: 105 a.a.

Struc: 77 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: 10.1038/emboj.2009.165

Embo J 28:2128-2142 (2009)

PubMed id: 19556970

Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner.

S.Sasso, M.Okvist, K.Roderer, M.Gamper, G.Codoni, U.Krengel, P.Kast.

ABSTRACT

Chorismate mutase catalyzes a key step in the shikimate biosynthetic pathway towards phenylalanine and tyrosine. Curiously, the intracellular chorismate mutase of Mycobacterium tuberculosis (MtCM; Rv0948c) has poor activity and lacks prominent active-site residues. However, its catalytic efficiency increases >100-fold on addition of DAHP synthase (MtDS; Rv2178c), another shikimate-pathway enzyme. The 2.35 A crystal structure of the MtCM-MtDS complex bound to a transition-state analogue shows a central core formed by four MtDS subunits sandwiched between two MtCM dimers. Structural comparisons imply catalytic activation to be a consequence of the repositioning of MtCM active-site residues on binding to MtDS. The mutagenesis of the C-terminal extrusion of MtCM establishes conserved residues as part of the activation machinery. The chorismate-mutase activity of the complex, but not of MtCM alone, is inhibited synergistically by phenylalanine and tyrosine. The complex formation thus endows the shikimate pathway of M. tuberculosis with an important regulatory feature. Experimental evidence suggests that such non-covalent enzyme complexes comprising an AroQ(delta) subclass chorismate mutase like MtCM are abundant in the bacterial order Actinomycetales.