2veq

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[[Image:2veq.jpg|left|200px]]
 
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{{Structure
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==Insights into kinetochore-DNA interactions from the structure of Cep3p==
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|PDB= 2veq |SIZE=350|CAPTION= <scene name='initialview01'>2veq</scene>, resolution 2.49&Aring;
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<StructureSection load='2veq' size='340' side='right'caption='[[2veq]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC2:Cac+Binding+Site+For+Chain+A'>AC2</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>
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<table><tr><td colspan='2'>[[2veq]] is a 1 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=2VEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VEQ FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.49&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene></td></tr>
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|DOMAIN=
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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=2veq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2veq OCA], [https://pdbe.org/2veq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2veq RCSB], [https://www.ebi.ac.uk/pdbsum/2veq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2veq ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2veq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2veq OCA], [http://www.ebi.ac.uk/pdbsum/2veq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2veq RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CBF3B_YEAST CBF3B_YEAST] Acts as a component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The CBF3 complex is an essential core component of the budding yeast kinetochore and is required for the centromeric localization of all other kinetochore proteins. We determined the crystal structure of a large section of the protein Cep3 from CBF3, which is the only component with obvious DNA-binding motifs. The protein adopts a roughly bilobal shape, with an extended dimerization interface. The dimer has a large central channel that is sufficient to accommodate duplex B-form DNA. The zinc-finger domains emerge at the edges of the channel, and could bind to the DNA in a pseudo-symmetrical manner at degenerate half-sites in the centromeric sequence. We propose a mechanism for the modulation of DNA affinity by an acidic activator domain, which could be applicable to a wider family of transcription factors.
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'''INSIGHTS INTO KINETOCHORE-DNA INTERACTIONS FROM THE STRUCTURE OF CEP3P'''
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Insights into kinetochore-DNA interactions from the structure of Cep3Delta.,Purvis A, Singleton MR EMBO Rep. 2008 Jan;9(1):56-62. Epub 2007 Dec 7. PMID:18064045<ref>PMID:18064045</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2veq" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The CBF3 complex is an essential core component of the budding yeast kinetochore and is required for the centromeric localization of all other kinetochore proteins. We determined the crystal structure of a large section of the protein Cep3 from CBF3, which is the only component with obvious DNA-binding motifs. The protein adopts a roughly bilobal shape, with an extended dimerization interface. The dimer has a large central channel that is sufficient to accommodate duplex B-form DNA. The zinc-finger domains emerge at the edges of the channel, and could bind to the DNA in a pseudo-symmetrical manner at degenerate half-sites in the centromeric sequence. We propose a mechanism for the modulation of DNA affinity by an acidic activator domain, which could be applicable to a wider family of transcription factors.
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*[[Centromere protein 3D structure|Centromere protein 3D structure]]
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== References ==
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==About this Structure==
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<references/>
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2VEQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VEQ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Insights into kinetochore-DNA interactions from the structure of Cep3Delta., Purvis A, Singleton MR, EMBO Rep. 2008 Jan;9(1):56-62. Epub 2007 Dec 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18064045 18064045]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Purvis A]]
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[[Category: Purvis, A.]]
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[[Category: Singleton MR]]
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[[Category: Singleton, M R.]]
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[[Category: cbf3 complex]]
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[[Category: cell cycle]]
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[[Category: centromere]]
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[[Category: cep3p]]
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[[Category: chromosomal protein]]
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[[Category: dna-binding]]
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[[Category: kinetochore]]
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[[Category: metal-binding]]
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[[Category: nucleus]]
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[[Category: phosphorylation]]
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[[Category: transcription factor]]
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[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:11:20 2008''
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Current revision

Insights into kinetochore-DNA interactions from the structure of Cep3p

PDB ID 2veq

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