1qsd: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[1qsd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QSD FirstGlance]. <br>
-</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=1qsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qsd OCA], [https://pdbe.org/1qsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qsd RCSB], [https://www.ebi.ac.uk/pdbsum/1qsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qsd ProSAT]</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]] 2.2&#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=1qsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qsd OCA], [https://pdbe.org/1qsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qsd RCSB], [https://www.ebi.ac.uk/pdbsum/1qsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qsd ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TBCA_YEAST TBCA_YEAST]] Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
+[https://www.uniprot.org/uniprot/TBCA_YEAST TBCA_YEAST] Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
 == 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=1qsd ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The folding pathway of tubulins includes highly specific interactions with a series of cofactors (A, B, C, D and E) after they are released from the eukaryotic chaperonin CCT. The 2.2 A crystal structure of Rbl2p, the Saccharomyces cerevisiae homolog of beta-tubulin specific cofactor A, shows alpha-helical monomers forming a flat, slightly convex dimer. The surface of the molecule is dominated by polar and charged residues and lacks hydrophobic patches typically observed for chaperones that bind unfolded or partially folded proteins. This post-chaperonin cofactor is therefore clearly distinct from typical chaperones where hydrophobicity is a hallmark of substrate recognition.
-Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p.,Steinbacher S Nat Struct Biol. 1999 Nov;6(11):1029-32. PMID:10542094<ref>PMID:10542094</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1qsd" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Steinbacher, S]]
+[[Category: Steinbacher S]]
-[[Category: Chaperone]]
-[[Category: Four-helix-bundle]]