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Expression, purification and crystallization of L-methionine gamma-lyase 2 from Entamoeba histolytica.

ABSTRACT: L-Methionine gamma-lyase (MGL) is considered to be an attractive target for rational drug development because the enzyme is absent in mammalian hosts. To enable structure-based design of drugs targeting MGL, one of the two MGL isoenzymes (EhMGL2) was crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 88.89, b = 102.68, c = 169.87 A. The crystal diffracted to a resolution of 2.0 A. The presence of a tetramer in the asymmetric unit (4 x 43.1 kDa) gives a Matthews coefficient of 2.2 A(3) Da(-1). The structure was solved by the molecular-replacement method and structure refinement is now in progress.

SUBMITTER: Sato D

PROVIDER: S-EPMC2225178 | biostudies-literature | 2006 Oct

REPOSITORIES: biostudies-literature

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Expression, purification and crystallization of L-methionine gamma-lyase 2 from Entamoeba histolytica.

Sato Dan D Yamagata Wataru W Kamei Kaeko K Nozaki Tomoyoshi T Harada Shigeharu S

Acta crystallographica. Section F, Structural biology and crystallization communications 20060930 Pt 10

L-Methionine gamma-lyase (MGL) is considered to be an attractive target for rational drug development because the enzyme is absent in mammalian hosts. To enable structure-based design of drugs targeting MGL, one of the two MGL isoenzymes (EhMGL2) was crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 88.89, b = 102.68, c = 169.87 A. The crystal diffracted to a resolution of 2.0 A. The presence of a tetramer in the asymmetric unit (4 x 43.1 kDa) gives a Matt ...[more]

PMID: 17012806

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