PDBsum entry: 2w19

Transferase/isomerase

PDB id: 2w19

Contents

Protein chains

419 a.a. *

72 a.a. *

75 a.a. *

Ligands

GOL ×11

SO4 ×3

Waters ×351

* Residue conservation analysis

PDB id:

2w19

Name:

Transferase/isomerase

Title:

Non-covalent complex between dahp synthase and chorismate mutase from mycobacterium tuberculosis

Structure:

3-deoxy-d-arabino-heptulosonate 7-phosphate synth chain: a, b. Synonym: dahp synthetase, phenylalanine-repressible. Engineered: yes. Chorismate mutase. Chain: c, d. Fragment: residues 16-105. Synonym: rv0948c/mt0975. Engineered: yes

Source:

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

Resolution:

2.15Å R-factor: 0.179 R-free: 0.211

Authors:

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

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:

16-Oct-08 Release date: 07-Jul-09

Protein chains

O53512  (O53512_MYCTU) -  Probable 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase AroG (DAHP synthetase, phenylalanine-repressible)

Seq: 462 a.a.

Struc: 419 a.a.

Protein chain

P64767  (Y948_MYCTU) -  Uncharacterized protein Rv0948c/MT0975

Seq: 105 a.a.

Struc: 72 a.a.

Protein chain

P64767  (Y948_MYCTU) -  Uncharacterized protein Rv0948c/MT0975

Seq: 105 a.a.

Struc: 75 a.a.

Enzyme reactions

• Enzyme class 2: Chains A, B: E.C.2.5.1.54 - 3-deoxy-7-phosphoheptulonate synthase.
• Pathway: Shikimate and Chorismate Biosynthesis
• Reaction: Phosphoenolpyruvate + D-erythrose 4-phosphate + H₂O = 3-deoxy-D- arabino-hept-2-ulosonate 7-phosphate + phosphate

Phosphoenolpyruvate + D-erythrose 4-phosphate (Bound ligand (Het Group name = GOL) matches with 50.00% similarity) + H(2)O = 3-deoxy-D- arabino-hept-2-ulosonate 7-phosphate + phosphate

• Enzyme class 3: Chains C, D: E.C.5.4.99.5 - Chorismate mutase.

Pathway:

• Reaction: Chorismate = prephenate

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

 Gene Ontology (GO) functional annotation 

• Cellular component: plasma membrane (2 terms)
• Biological process: growth (6 terms)
• Biochemical function: protein binding (5 terms)

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.