Crystallization of the C-terminal domain of the mouse brain cytosolic long-chain acyl-CoA thioesterase.
The mammalian long-chain acyl-CoA thioesterase, the enzyme that catalyses the hydrolysis of acyl-CoAs to free fatty acids, contains two fused 4HBT (4-hydroxybenzoyl-CoA thioesterase) motifs. The C-terminal domain of the mouse long-chain acyl-CoA thioesterase (Acot7) has been expressed in bacteria and crystallized. The crystals were obtained by vapour diffusion using PEG 2000 MME as precipitant at pH 7.0 and 290 K. The crystals have the symmetry of space group R32 (unit-cell parameters a = b = 136.83, c = 99.82 A, gamma = 120 degrees). Two molecules are expected in the asymmetric unit. The crystals diffract to 2.4 A resolution using the laboratory X-ray source and are suitable for crystal structure determination.
Serek
Robert
R
School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Queensland 4072, Australia.
Forwood
Jade K
JK
Hume
David A
DA
Martin
Jennifer L
JL
Kobe
Bostjan
B
D000818:Animals; D001921:Brain / Q000201:enzymology*; D043182:Carboxylesterase / Q000737:chemistry; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003600:Cytosol / Q000201:enzymology; D051379:Mice; D013869:Thiolester Hydrolases / Q000737:chemistry
D002265:Carboxylic Ester Hydrolases; C063418:long-chain carboxylesterase; D043182:Carboxylesterase; D013869:Thiolester Hydrolases