2veq
From Proteopedia
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|PDB= 2veq |SIZE=350|CAPTION= <scene name='initialview01'>2veq</scene>, resolution 2.49Å | |PDB= 2veq |SIZE=350|CAPTION= <scene name='initialview01'>2veq</scene>, resolution 2.49Å | ||
|SITE= <scene name='pdbsite=AC2:Cac+Binding+Site+For+Chain+A'>AC2</scene> | |SITE= <scene name='pdbsite=AC2:Cac+Binding+Site+For+Chain+A'>AC2</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Purvis, A.]] | [[Category: Purvis, A.]] | ||
[[Category: Singleton, M R.]] | [[Category: Singleton, M R.]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: CAC]] | ||
[[Category: cbf3 complex]] | [[Category: cbf3 complex]] | ||
[[Category: cell cycle]] | [[Category: cell cycle]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:11:20 2008'' |
Revision as of 02:11, 31 March 2008
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| , resolution 2.49Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
INSIGHTS INTO KINETOCHORE-DNA INTERACTIONS FROM THE STRUCTURE OF CEP3P
Overview
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.
About this Structure
2VEQ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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
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