1np2

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|SITE=
|SITE=
|LIGAND=
|LIGAND=
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1np2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1np2 OCA], [http://www.ebi.ac.uk/pdbsum/1np2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1np2 RCSB]</span>
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[[Category: tim barrel]]
[[Category: tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:33:29 2008''

Revision as of 19:33, 30 March 2008


PDB ID 1np2

Drag the structure with the mouse to rotate
, resolution 2.4Å
Activity: Beta-glucosidase, with EC number 3.2.1.21
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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