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Crystallization of an apo form of human arginase: using all the tools in the toolbox simultaneously.

ABSTRACT: Arginase (EC 3.5.3.1) is an aminohydrolase that acts on L-arginine to produce urea and ornithine. Two isotypes of the enzyme are found in humans. Type I is predominantly produced in the liver and is a homotrimer of 35?kDa subunits. Human arginase (hArginase) I is seen to be up-regulated in many diseases and is a potential therapeutic target for many diverse indications. Previous reports of crystallization and structure determination of hArginase have always included inhibitors of the enzyme: here, the first case of a true apo crystal form of the enzyme which is suitable for small-molecule soaking is reported. The crystals belonged to space group P2(1)2(1)2(1) and have approximate unit-cell parameters a=53, b=67.5, c=250?Å. The crystals showed slightly anisotropic diffraction to beyond 2.0?Å resolution.

SUBMITTER: Newman J

PROVIDER: S-EPMC3079981 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Crystallization of an apo form of human arginase: using all the tools in the toolbox simultaneously.

Newman Janet J Pearce Lesley L Lesburg Charles A CA Strickland Corey C Peat Thomas S TS

Acta crystallographica. Section F, Structural biology and crystallization communications 20101223 Pt 1

Arginase (EC 3.5.3.1) is an aminohydrolase that acts on L-arginine to produce urea and ornithine. Two isotypes of the enzyme are found in humans. Type I is predominantly produced in the liver and is a homotrimer of 35 kDa subunits. Human arginase (hArginase) I is seen to be up-regulated in many diseases and is a potential therapeutic target for many diverse indications. Previous reports of crystallization and structure determination of hArginase have always included inhibitors of the enzyme: her ...[more]

PMID: 21206033

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