Crystal structure of a putative acyl-CoA thioesterase from Xanthomonas campestris (XC229) adopts a tetrameric hotdog fold of epsilongamma mode

Proteins. 2006 Aug 15;64(3):823-6. doi: 10.1002/prot.21037.

Authors

Ko-Hsin Chin¹, Chia-Cheng Chou, Andrew H-J Wang, Shan-Ho Chou

Affiliation

¹ Institute of Biochemistry, National Chung-Hsing University, Taichung, Taiwan, Republic of China.

PMID: 16763992
DOI: 10.1002/prot.21037

No abstract available

Publication types

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

MeSH terms

Amino Acid Sequence
Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Bacterial Proteins / metabolism
Binding Sites / genetics
Crystallization
Crystallography, X-Ray / methods*
Models, Molecular
Molecular Sequence Data
Palmitoyl-CoA Hydrolase / chemistry*
Palmitoyl-CoA Hydrolase / genetics
Palmitoyl-CoA Hydrolase / metabolism
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Substrate Specificity
Xanthomonas campestris / genetics
Xanthomonas campestris / metabolism*

Substances

Bacterial Proteins
Palmitoyl-CoA Hydrolase