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1sce

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[[Image:1sce.gif|left|200px]]
 
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==CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN SUC1 REVEALS A NOVEL BETA-HINGE CONFORMATIONAL SWITCH==
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The line below this paragraph, containing "STRUCTURE_1sce", creates the "Structure Box" on the page.
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<StructureSection load='1sce' size='340' side='right'caption='[[1sce]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1sce]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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{{STRUCTURE_1sce| PDB=1sce | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sce OCA], [https://pdbe.org/1sce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sce RCSB], [https://www.ebi.ac.uk/pdbsum/1sce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sce ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CKS1_SCHPO CKS1_SCHPO] Binds to the catalytic subunit of the cyclin dependent kinase (cdc2) and is essential for its biological function.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sc/1sce_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1sce ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN SUC1 REVEALS A NOVEL BETA-HINGE CONFORMATIONAL SWITCH'''
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==See Also==
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*[[Cyclin-dependent kinase regulatory subunit 3D structures|Cyclin-dependent kinase regulatory subunit 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The Schizosaccharomyces pombe cell cycle-regulatory protein suc1, named as the suppressor of cdc2 temperature-sensitive mutations, is essential for cell cycle progression. To understand suc1 structure-function relationships and to help resolve conflicting interpretations of suc1 function based on genetic studies of suc1 and its functional homologs in both lower and higher eukaryotes, we have determined the crystal structure of the beta-interchanged suc1 dimer. Each domain consists of three alpha-helices and a four-stranded beta-sheet, completed by the interchange of terminal beta-strands between the two subunits. This beta-interchanged suc1 dimer, when compared with the beta-hairpin single-domain folds of suc1, reveals a beta-hinge motif formed by the conserved amino acid sequence HVPEPH. This beta-hinge mediates the subunit conformation and assembly of suc1: closing produces the intrasubunit beta-hairpin and single-domain fold, whereas opening leads to the intersubunit beta-strand interchange and interlocked dimer assembly reported here. This conformational switch markedly changes the surface accessibility of sequence-conserved residues available for recognition of cyclin-dependent kinase, suggesting a structural mechanism for beta-hinge-mediated regulation of suc1 biological function. Thus, suc1 belongs to the family of domain-swapping proteins, consisting of intertwined and dimeric protein structures in which the dual assembly modes regulate their function.
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[[Category: Large Structures]]
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==About this Structure==
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1SCE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCE OCA].
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==Reference==
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Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch., Bourne Y, Arvai AS, Bernstein SL, Watson MH, Reed SI, Endicott JE, Noble ME, Johnson LN, Tainer JA, Proc Natl Acad Sci U S A. 1995 Oct 24;92(22):10232-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7479758 7479758]
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[[Category: Schizosaccharomyces pombe]]
[[Category: Schizosaccharomyces pombe]]
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[[Category: Single protein]]
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[[Category: Bourne Y]]
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[[Category: Bourne, Y.]]
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[[Category: Tainer JA]]
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[[Category: Tainer, J A.]]
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[[Category: Cell cycle regulatory protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:32:33 2008''
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Current revision

CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN SUC1 REVEALS A NOVEL BETA-HINGE CONFORMATIONAL SWITCH

PDB ID 1sce

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