1np2: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1np2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_nonproteolyticus Thermus nonproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NP2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1np2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_nonproteolyticus Thermus nonproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NP2 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1np2 RCSB], [http://www.ebi.ac.uk/pdbsum/1np2 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1np2 RCSB], [http://www.ebi.ac.uk/pdbsum/1np2 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Beta-glucosidase]] | [[Category: Beta-glucosidase]] | ||
[[Category: Thermus nonproteolyticus]] | [[Category: Thermus nonproteolyticus]] | ||
[[Category: Chang, W R | [[Category: Chang, W R]] | ||
[[Category: He, X Y | [[Category: He, X Y]] | ||
[[Category: Liang, D C | [[Category: Liang, D C]] | ||
[[Category: Wang, X Q | [[Category: Wang, X Q]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Tim barrel]] | [[Category: Tim barrel]] | ||
Revision as of 19:42, 5 January 2015
Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium Thermus nonproteolyticus HG102Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium Thermus nonproteolyticus HG102
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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