1np2: Difference between revisions

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<StructureSection load='1np2' size='340' side='right'caption='[[1np2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1np2' size='340' side='right'caption='[[1np2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1np2]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1NP2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1np2]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1NP2 FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1np2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1np2 OCA], [https://pdbe.org/1np2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1np2 RCSB], [https://www.ebi.ac.uk/pdbsum/1np2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1np2 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1np2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1np2 OCA], [https://pdbe.org/1np2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1np2 RCSB], [https://www.ebi.ac.uk/pdbsum/1np2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1np2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9L794_9DEIN Q9L794_9DEIN]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus nonproteolyticus]]
[[Category: Thermus nonproteolyticus]]
[[Category: Beta-glucosidase]]
[[Category: Chang WR]]
[[Category: Large Structures]]
[[Category: He XY]]
[[Category: Chang, W R]]
[[Category: Liang DC]]
[[Category: He, X Y]]
[[Category: Wang XQ]]
[[Category: Liang, D C]]
[[Category: Wang, X Q]]
[[Category: Hydrolase]]
[[Category: Tim barrel]]

Latest revision as of 10:20, 25 October 2023

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

1np2 is a 2 chain structure with sequence from Thermus nonproteolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9L794_9DEIN

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 PubMed

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.

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

  1. Wang X, He X, Yang S, An X, Chang W, Liang D. Structural basis for thermostability of beta-glycosidase from the thermophilic eubacterium Thermus nonproteolyticus HG102. J Bacteriol. 2003 Jul;185(14):4248-55. PMID:12837801

1np2, resolution 2.40Å

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OCA