1gow: Difference between revisions

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 <StructureSection load='1gow' size='340' side='right'caption='[[1gow]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gow]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GOW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1gow]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GOW FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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]] 2.6&#8491;</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=1gow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gow OCA], [http://pdbe.org/1gow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gow RCSB], [http://www.ebi.ac.uk/pdbsum/1gow PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gow 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=1gow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gow OCA], [https://pdbe.org/1gow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gow RCSB], [https://www.ebi.ac.uk/pdbsum/1gow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gow ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/BGAL_SACS2 BGAL_SACS2]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1gow ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Enzymes from hyperthermophilic organisms must operate at temperatures which rapidly denature proteins from mesophiles. The structural basis of this thermostability is still poorly understood. Towards a further understanding of hyperthermostability, we have determined the crystal structure of the beta-glycosidase (clan GH-1A, family 1) from the hyperthermophilic archaeon Sulfolobus solfataricus at 2.6 A resolution. The enzyme is a tetramer with subunit molecular mass at 60 kDa, and crystallises with half of the tetramer in the asymmetric unit. The structure is a (betaalpha)8 barrel, but with substantial elaborations between the beta-strands and alpha-helices in each repeat. The active site occurs at the centre of the top face of the barrel and is connected to the surface by a radial channel which becomes a blind-ended tunnel in the tetramer, and probably acts as the binding site for extended oligosaccharide substrates. Analysis of the structure reveals two features which differ significantly from mesophile proteins; (1) an unusually large proportion of surface ion-pairs involved in networks that cross-link sequentially separate structures on the protein surface, and (2) an unusually large number of solvent molecules buried in hydrophilic cavities between sequentially separate structures in the protein core. These factors suggest a model for hyperthermostability via resilience rather than rigidity.
-Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability.,Aguilar CF, Sanderson I, Moracci M, Ciaramella M, Nucci R, Rossi M, Pearl LH J Mol Biol. 1997 Sep 5;271(5):789-802. PMID:9299327<ref>PMID:9299327</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1gow" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Galactosidase 3D structures|Galactosidase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Beta-galactosidase]]
 [[Category: Large Structures]]
-[[Category: Sulfolobus solfataricus]]
+[[Category: Saccharolobus solfataricus]]
-[[Category: Aguilar, C F]]
+[[Category: Aguilar CF]]
-[[Category: Pearl, L H]]
+[[Category: Pearl LH]]
-[[Category: Sanderson, I]]
+[[Category: Sanderson I]]
-[[Category: Beta-glycosidase]]
-[[Category: Hydrolase]]