1gon: Difference between revisions

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-==B-GLUCOSIDASE FROM STREPTOMYCES SP==
-<StructureSection load='1gon' size='340' side='right' caption='[[1gon]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+==b-glucosidase from Streptomyces sp==
+<StructureSection load='1gon' size='340' side='right'caption='[[1gon]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gon]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chainia_sp. Chainia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GON FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1gon]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GON FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gnx|1gnx]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1gon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gon OCA], [http://pdbe.org/1gon PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gon RCSB], [http://www.ebi.ac.uk/pdbsum/1gon PDBsum]</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=1gon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gon OCA], [https://pdbe.org/1gon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gon RCSB], [https://www.ebi.ac.uk/pdbsum/1gon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gon ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q59976_STRSQ Q59976_STRSQ]
 == 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/go/1gon_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/go/1gon_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1gon ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-An intracellular beta-glucosidase (Bgl3) from Streptomyces sp. has been cloned and overexpressed in Escherichia coli. The introduction of a His tag at the N-terminal end of the protein has allowed its purification to homogeneity by a single chromatographic step, with yields of 150-200 mg of pure protein per litre of E. coli culture. The enzyme (52.6 kDa) is a retaining glycosidase able to hydrolyze a wide range of disaccharides and oligosaccharides and to perform transglycosylation. Crystals of recombinant Bgl3 have been grown from an ammonium sulfate solution using the hanging-drop vapour-diffusion method at 293 K. The crystals belong to the orthorhombic space group I222 with unit-cell dimensions a = 101.6, b = 113.4 and c = 187.5 A at room temperature and contain two molecules per asymmetric unit. A full 1.69 A resolution diffraction data set (97.7% completeness) has been collected from frozen crystals in a solution containing 30% sucrose, using synchrotron radiation.
-Cloning, overexpression, crystallization and preliminary X-ray analysis of a family 1 beta--glucosidase from Streptomyces.,Guasch A, Vallmitjana M, Perez R, Querol E, Perez-Pons JA, Coll M Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):679-82. PMID:10089468<ref>PMID:10089468</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1gon" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Beta-glucosidase|Beta-glucosidase]]
+*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Chainia sp]]
+[[Category: Large Structures]]
-[[Category: Coll, M]]
+[[Category: Streptomyces sp]]
-[[Category: Guasch, A]]
+[[Category: Coll M]]
-[[Category: Perez-Pons, J A]]
+[[Category: Guasch A]]
-[[Category: Querol, E]]
+[[Category: Perez-Pons JA]]
-[[Category: Vallmitjana, M]]
+[[Category: Querol E]]
-[[Category: Family 1 of glycosyl hydrolase]]
+[[Category: Vallmitjana M]]
-[[Category: Glycosyltransferase]]
-[[Category: Hydrolase]]