1qb3: Difference between revisions

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 <StructureSection load='1qb3' size='340' side='right'caption='[[1qb3]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qb3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QB3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qb3]] is a 3 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=1QB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QB3 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=1qb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qb3 OCA], [https://pdbe.org/1qb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qb3 RCSB], [https://www.ebi.ac.uk/pdbsum/1qb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qb3 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]] 3&#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=1qb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qb3 OCA], [https://pdbe.org/1qb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qb3 RCSB], [https://www.ebi.ac.uk/pdbsum/1qb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qb3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CKS1_YEAST CKS1_YEAST]] Binds to the catalytic subunit of the cyclin dependent kinase (CDC28) and is essential for its biological function.
+[https://www.uniprot.org/uniprot/CKS1_YEAST CKS1_YEAST] Binds to the catalytic subunit of the cyclin dependent kinase (CDC28) and is essential for its biological function.
 == 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=1qb3 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-BACKGROUND: The Saccharomyces cerevisiae protein Cks1 (cyclin-dependent kinase subunit 1) is essential for cell-cycle progression. The biological function of Cks1 can be modulated by a switch between two distinct molecular assemblies: the single domain fold, which results from the closing of a beta-hinge motif, and the intersubunit beta-strand interchanged dimer, which arises from the opening of the beta-hinge motif. The crystal structure of a cyclin-dependent kinase (Cdk) in complex with the human Cks homolog CksHs1 single-domain fold revealed the importance of conserved hydrophobic residues and charged residues within the beta-hinge motif. RESULTS: The 3.0 A resolution Cks1 structure reveals the strict structural conservation of the Cks alpha/beta-core fold and the beta-hinge motif. The beta hinge identified in the Cks1 structure includes a novel pivot and exposes a cluster of conserved tyrosine residues that are involved in Cdk binding but are sequestered in the beta-interchanged Cks homolog suc1 dimer structure. This Cks1 structure confirms the conservation of the Cks anion-binding site, which interacts with sidechain residues from the C-terminal alpha helix of another subunit in the crystal. CONCLUSIONS: The Cks1 structure exemplifies the conservation of the beta-interchanged dimer and the anion-binding site in evolutionarily distant yeast and human Cks homologs. Mutational analyses including in vivo rescue of CKS1 disruption support the dual functional roles of the beta-hinge residue Glu94, which participates in Cdk binding, and of the anion-binding pocket that is located 22 A away and on an opposite face to Glu94. The Cks1 structure suggests a biological role for the beta-interchanged dimer and the anion-binding site in targeting Cdks to specific phosphoproteins during cell-cycle progression.
-Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions.,Bourne Y, Watson MH, Arvai AS, Bernstein SL, Reed SI, Tainer JA Structure. 2000 Aug 15;8(8):841-50. PMID:10997903<ref>PMID:10997903</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1qb3" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Cyclin-dependent kinase regulatory subunit 3D structures|Cyclin-dependent kinase regulatory subunit 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Arvai, A S]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Bernstein, S L]]
+[[Category: Arvai AS]]
-[[Category: Bourne, Y]]
+[[Category: Bernstein SL]]
-[[Category: Reed, S I]]
+[[Category: Bourne Y]]
-[[Category: Tainer, J A]]
+[[Category: Reed SI]]
-[[Category: Watson, M H]]
+[[Category: Tainer JA]]
-[[Category: Cell cycle]]
+[[Category: Watson MH]]
-[[Category: Cell cycle mutagenesis domain swapping]]
-[[Category: Cyclin-dependent kinase]]