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

Ye Yuan; Xiao Wang; Xu Li; Maikun Teng; Liwen Niu; Yongxiang Gao

doi:10.1107/S1744309112019276

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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):775-7. doi: 10.1107/S1744309112019276. Epub 2012 Jun 27.

Authors

Ye Yuan¹, Xiao Wang, Xu Li, Maikun Teng, Liwen Niu, Yongxiang Gao

Affiliation

¹ Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Chromatography, Gel
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Saccharomyces cerevisiae / enzymology*
Saccharomyces cerevisiae Proteins / chemistry*
Saccharomyces cerevisiae Proteins / genetics
Saccharomyces cerevisiae Proteins / isolation & purification
Thiolester Hydrolases / chemistry*
Thiolester Hydrolases / genetics
Thiolester Hydrolases / isolation & purification

Substances

Saccharomyces cerevisiae Proteins
Thiolester Hydrolases
YLR118C protein, S cerevisiae