Crystal structure of an acetyl esterase complexed with acetate ion provides insights into the catalytic mechanism
| Autor: | Masahiro Watanabe, Shouhei Mine, Keiko Uechi, Saori Kamachi, Hironaga Akita |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Stereochemistry Biophysics Crystal structure Acetates Crystallography X-Ray Biochemistry Esterase Article Catalysis Substrate Specificity RMSD root mean square deviation 03 medical and health sciences Catalytic triad Molecule Amino Acid Sequence Molecular Biology Carbohydrate esterase family 3 CE carbohydrate esterase 030102 biochemistry & molecular biology biology Sequence Homology Amino Acid Hydrogen bond Chemistry Acetyl esterase Talaromyces cellulolyticus Active site Cell Biology TcAE206 the catalytic domain of acetylesterase from Talaromyces cellulolyticus SGNH-hydrolase S10A mutant of TcAE206 substituted serine 10 with alanine 030104 developmental biology Oxyanion hole Sm23 acetylxylan esterase from Sinorhizobium meliloti Talaromyces biology.protein CtCes3-1 acetylxylan esterase from Clostridium thermocellum Acetylesterase |
| Zdroj: | Biochemical and Biophysical Research Communications |
| ISSN: | 1090-2104 0006-291X |
| Popis: | We previously reported the crystal structure of an acetyl esterase (TcAE206) belonging to carbohydrate esterase family 3 from Talaromyces cellulolyticus. In this study, we solved the crystal structure of an S10A mutant of TcAE206 complexed with an acetate ion. The acetate ion was stabilized by three hydrogen bonds in the oxyanion hole instead of a water molecule as in the structure of wild-type TcAE206. Furthermore, the catalytic triad residue His182 moved 0.8 Å toward the acetate ion upon substrate entering the active site, suggesting that this movement is necessary for completion of the catalytic reaction. Highlights • The crystal structure of TcAE206_S10A with acetate ion was solved at 1.4 Å resolution. • The complex structure revealed the catalytic mechanism. • His182, which moves 0.8 Å toward the acetate ion, is necessary for enzymatic activity. • This study provides insights into the substrate specificity of fungal CE3 enzymes. |
| Databáze: | OpenAIRE |
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