This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wang, X.
Right arrow Articles by Liang, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wang, X.
Right arrow Articles by Liang, D.

 Previous Article  |  Next Article 

Journal of Bacteriology, July 2003, p. 4248-4255, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4248-4255.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Structural Basis for Thermostability of ß-Glycosidase from the Thermophilic Eubacterium Thermus nonproteolyticus HG102

Xinquan Wang,1 Xiangyuan He,2 Shoujun Yang,2 Xiaomin An,1 Wenrui Chang,1 and Dongcai Liang1*

National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101,1 Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, People's Republic of China2

Received 24 January 2003/ Accepted 28 April 2003

The three-dimensional structure of a thermostable ß-glycosidase (GlyTn) from the thermophilic eubacterium Thermus nonproteolyticus HG102 was determined at a resolution of 2.4 Å. The core of the structure adopts the (ß{alpha})8 barrel fold. The sequence alignments and the positions of the two Glu residues in the active center indicate that GlyTn belongs to the glycosyl hydrolases of retaining family 1. We have analyzed the structural features of GlyTn related to the thermostability and compared its structure with those of other mesophilic glycosidases from plants, eubacteria, and hyperthermophilic enzymes from archaea. Several possible features contributing to the thermostability of GlyTn were elucidated.

* Corresponding author. Mailing address: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Rd., Beijing 100101, People's Republic of China. Phone: 86-10-64888506. Fax: 86-10-64889867. E-mail: dcliang{at}sun5.ibp.ac.cn.

Journal of Bacteriology, July 2003, p. 4248-4255, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4248-4255.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Miyake, R., Kawamoto, J., Wei, Y.-L., Kitagawa, M., Kato, I., Kurihara, T., Esaki, N. (2007). Construction of a Low-Temperature Protein Expression System Using a Cold-Adapted Bacterium, Shewanella sp. Strain Ac10, as the Host. Appl. Environ. Microbiol. 73: 4849-4856 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»