title: Crystal structure of a putative acyl-CoA thioesterase from Xanthomonas campestris (XC229) adopts a tetrameric hotdog fold of epsilongamma mode.
authors.affiliation: Institute of Biochemistry, National Chung-Hsing University, Taichung, Taiwan, Republic of China.
authors.forename: Ko-Hsin
authors.initials: KH
authors.lastname: Chin
authors.forename: Chia-Cheng
authors.initials: CC
authors.lastname: Chou
authors.forename: Andrew H-J
authors.initials: AH
authors.lastname: Wang
authors.forename: Shan-Ho
authors.initials: SH
authors.lastname: Chou
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010170:Palmitoyl-CoA Hydrolase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D016959:Xanthomonas campestris / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D010170:Palmitoyl-CoA Hydrolase