1np2: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1np2.gif|left|200px]]<br /><applet load="1np2" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1np2, resolution 2.4&Aring;" />
-'''Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium Thermus nonproteolyticus HG102'''<br />
-==Overview==
+==Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium Thermus nonproteolyticus HG102==
-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.
+<StructureSection load='1np2' size='340' side='right'caption='[[1np2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== 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>
+</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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9L794_9DEIN Q9L794_9DEIN]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/np/1np2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1np2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==About this Structure==
+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<ref>PMID:12837801</ref>
-NP2 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NP2 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12837801 12837801]
+</div>
-[[Category: Beta-glucosidase]]
+<div class="pdbe-citations 1np2" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Thermus nonproteolyticus]]
-[[Category: Chang, W.R.]]
+[[Category: Chang WR]]
-[[Category: He, X.Y.]]
+[[Category: He XY]]
-[[Category: Liang, D.C.]]
+[[Category: Liang DC]]
-[[Category: Wang, X.Q.]]
+[[Category: Wang XQ]]
-[[Category: tim barrel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:30:58 2007''