1np2
From Proteopedia
(New page: 200px<br /><applet load="1np2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1np2, resolution 2.4Å" /> '''Crystal structure of ...) |
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| - | [[Image:1np2.gif|left|200px]]<br /><applet load="1np2" size=" | + | [[Image:1np2.gif|left|200px]]<br /><applet load="1np2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1np2, resolution 2.4Å" /> | caption="1np2, resolution 2.4Å" /> | ||
'''Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium Thermus nonproteolyticus HG102'''<br /> | '''Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium Thermus nonproteolyticus HG102'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of a thermostable beta-glycosidase | + | The three-dimensional structure of a thermostable beta-glycosidase (Gly(Tn)) from the thermophilic eubacterium Thermus nonproteolyticus HG102 was determined at a resolution of 2.4 A. The core of the structure adopts the (betaalpha)(8) barrel fold. The sequence alignments and the positions of the two Glu residues in the active center indicate that Gly(Tn) belongs to the glycosyl hydrolases of retaining family 1. We have analyzed the structural features of Gly(Tn) 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 Gly(Tn) were elucidated. |
==About this Structure== | ==About this Structure== | ||
| - | 1NP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_nonproteolyticus Thermus nonproteolyticus]. Active as [http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] Full crystallographic information is available from [http:// | + | 1NP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_nonproteolyticus Thermus nonproteolyticus]. Active as [http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NP2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus nonproteolyticus]] | [[Category: Thermus nonproteolyticus]] | ||
| - | [[Category: Chang, W | + | [[Category: Chang, W R.]] |
| - | [[Category: He, X | + | [[Category: He, X Y.]] |
| - | [[Category: Liang, D | + | [[Category: Liang, D C.]] |
| - | [[Category: Wang, X | + | [[Category: Wang, X Q.]] |
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:26 2008'' |
Revision as of 12:08, 21 February 2008
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Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium Thermus nonproteolyticus HG102
Overview
The three-dimensional structure of a thermostable beta-glycosidase (Gly(Tn)) from the thermophilic eubacterium Thermus nonproteolyticus HG102 was determined at a resolution of 2.4 A. The core of the structure adopts the (betaalpha)(8) barrel fold. The sequence alignments and the positions of the two Glu residues in the active center indicate that Gly(Tn) belongs to the glycosyl hydrolases of retaining family 1. We have analyzed the structural features of Gly(Tn) 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 Gly(Tn) were elucidated.
About this Structure
1NP2 is a Single protein structure of sequence from Thermus nonproteolyticus. Active as Beta-glucosidase, with EC number 3.2.1.21 Full crystallographic information is available from OCA.
Reference
Structural basis for thermostability of beta-glycosidase from the thermophilic eubacterium Thermus nonproteolyticus HG102., Wang X, He X, Yang S, An X, Chang W, Liang D, J Bacteriol. 2003 Jul;185(14):4248-55. PMID:12837801
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