1sce: Difference between revisions

New page: left|200px<br /><applet load="1sce" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sce, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1sce.gif|left|200px]]<br /><applet load="1sce" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1sce, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN SUC1 REVEALS A NOVEL BETA-HINGE CONFORMATIONAL SWITCH'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN SUC1 REVEALS A NOVEL BETA-HINGE CONFORMATIONAL SWITCH==
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.
<StructureSection load='1sce' size='340' side='right'caption='[[1sce]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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>
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=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>
</table>
== Function ==
[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.
== 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/sc/1sce_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/main_output.php?pdb_ID=1sce ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1SCE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SCE OCA].
*[[Cyclin-dependent kinase regulatory subunit 3D structures|Cyclin-dependent kinase regulatory subunit 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7479758 7479758]
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Single protein]]
[[Category: Bourne Y]]
[[Category: Bourne, Y.]]
[[Category: Tainer JA]]
[[Category: Tainer, J.A.]]
[[Category: CL]]
[[Category: cell cycle regulatory protein]]
 
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