2bc3: Difference between revisions

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 ==T7-tagged full-length streptavidin==
-<StructureSection load='2bc3' size='340' side='right' caption='[[2bc3]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
+<StructureSection load='2bc3' size='340' side='right'caption='[[2bc3]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bc3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1583 As 4.1583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BC3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bc3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BC3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.54&#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=2bc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bc3 OCA], [http://pdbe.org/2bc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bc3 RCSB], [http://www.ebi.ac.uk/pdbsum/2bc3 PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[https://proteopedia.org/fgij/fg.htm?mol=2bc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bc3 OCA], [https://pdbe.org/2bc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bc3 RCSB], [https://www.ebi.ac.uk/pdbsum/2bc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bc3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV]] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
+[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
 == 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/bc/2bc3_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/2bc3_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 18: / Line 20: @@
 </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=2bc3 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The structure of a full-length streptavidin has been determined at 1.7 A resolution and shows that the 20 residue extension at the C terminus forms a well-ordered polypeptide loop on the surface of the tetramer. Residues 150-153 of the extension are bound to the ligand-binding site, possibly competing with exogenous ligands. The binding mode of these residues is compared with that of biotin and peptidic ligands. The observed structure helps to rationalize the observations that full-length mature streptavidin binds biotinylated macromolecules with reduced affinity.
-Crystallographic analysis of a full-length streptavidin with its C-terminal polypeptide bound in the biotin binding site.,Le Trong I, Humbert N, Ward TR, Stenkamp RE J Mol Biol. 2006 Feb 24;356(3):738-45. Epub 2005 Dec 15. PMID:16384581<ref>PMID:16384581</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2bc3" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Avidin|Avidin]]
+*[[Avidin 3D structures|Avidin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: As 4 1583]]
+[[Category: Large Structures]]
-[[Category: Humbert, N]]
+[[Category: Streptomyces avidinii]]
-[[Category: Stenkamp, R E]]
+[[Category: Humbert N]]
-[[Category: Trong, I Le]]
+[[Category: Le Trong I]]
-[[Category: Ward, T R]]
+[[Category: Stenkamp RE]]
-[[Category: Biotin binding protein]]
+[[Category: Ward TR]]
-[[Category: Streptavidin]]
-[[Category: T7 tag]]