Unknown

Dataset Information

0

A novel noncovalent complex of chorismate mutase and DAHP synthase from Mycobacterium tuberculosis: protein purification, crystallization and X-ray diffraction analysis.


ABSTRACT: Chorismate mutase catalyzes a key step in the shikimate-biosynthetic pathway and hence is an essential enzyme in bacteria, plants and fungi. Mycobacterium tuberculosis contains two chorismate mutases, a secreted and an intracellular one, the latter of which (MtCM; Rv0948c; 90 amino-acid residues; 10 kDa) is the subject of this work. Here are reported the gene expression, purification and crystallization of MtCM alone and of its complex with another shikimate-pathway enzyme, DAHP synthase (MtDS; Rv2178c; 472 amino-acid residues; 52 kDa), which has been shown to enhance the catalytic efficiency of MtCM. The MtCM-MtDS complex represents the first noncovalent enzyme complex from the common shikimate pathway to be structurally characterized. Soaking experiments with a transition-state analogue are also reported. The crystals of MtCM and the MtCM-MtDS complex diffracted to 1.6 and 2.1 A resolution, respectively.

SUBMITTER: Okvist M 

PROVIDER: S-EPMC2765898 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

A novel noncovalent complex of chorismate mutase and DAHP synthase from Mycobacterium tuberculosis: protein purification, crystallization and X-ray diffraction analysis.

Okvist Mats M   Sasso Severin S   Roderer Kathrin K   Kast Peter P   Krengel Ute U  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090925 Pt 10


Chorismate mutase catalyzes a key step in the shikimate-biosynthetic pathway and hence is an essential enzyme in bacteria, plants and fungi. Mycobacterium tuberculosis contains two chorismate mutases, a secreted and an intracellular one, the latter of which (MtCM; Rv0948c; 90 amino-acid residues; 10 kDa) is the subject of this work. Here are reported the gene expression, purification and crystallization of MtCM alone and of its complex with another shikimate-pathway enzyme, DAHP synthase (MtDS;  ...[more]

Similar Datasets

| S-EPMC3370916 | biostudies-literature
| S-EPMC2219981 | biostudies-literature
| S-EPMC2718287 | biostudies-literature
| S-EPMC2222579 | biostudies-literature
| S-EPMC3943096 | biostudies-literature
| S-EPMC2243083 | biostudies-literature
| S-EPMC2374160 | biostudies-literature
| S-EPMC4909250 | biostudies-literature
| S-EPMC3660905 | biostudies-literature
| S-EPMC2374159 | biostudies-literature