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Cloning, purification, crystallization and preliminary X-ray diffraction crystallographic study of acyl-protein thioesterase 1 from Saccharomyces cerevisiae.

ABSTRACT: Palmitoylation/depalmitoylation plays an important role in protein modification. yApt1 is the only enzyme in Saccharomyces cerevisiae that catalyses depalmitoylation. In the present study, recombinant full-length yApt1 was cloned, expressed, purified and crystallized. The crystals diffracted to 2.40?Å resolution and belonged to space group P4(2)2(1)2, with unit-cell parameters a = b = 146.43, c = 93.29?Å. A preliminary model of the three-dimensional structure has been built and further refinement is ongoing.

SUBMITTER: Yuan Y

PROVIDER: S-EPMC3388919 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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Cloning, purification, crystallization and preliminary X-ray diffraction crystallographic study of acyl-protein thioesterase 1 from Saccharomyces cerevisiae.

Yuan Ye Y Wang Xiao X Li Xu X Teng Maikun M Niu Liwen L Gao Yongxiang Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20120627 Pt 7

Palmitoylation/depalmitoylation plays an important role in protein modification. yApt1 is the only enzyme in Saccharomyces cerevisiae that catalyses depalmitoylation. In the present study, recombinant full-length yApt1 was cloned, expressed, purified and crystallized. The crystals diffracted to 2.40 Å resolution and belonged to space group P4(2)2(1)2, with unit-cell parameters a = b = 146.43, c = 93.29 Å. A preliminary model of the three-dimensional structure has been built and further refinemen ...[more]

PMID: 22750862

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