2bym
From Proteopedia
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| - | [[Image:2bym.gif|left|200px]]<br /> | + | [[Image:2bym.gif|left|200px]]<br /><applet load="2bym" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2bym" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2bym, resolution 2.80Å" /> | caption="2bym, resolution 2.80Å" /> | ||
'''HISTONE FOLD HETERODIMER OF THE CHROMATIN ACCESSIBILITY COMPLEX'''<br /> | '''HISTONE FOLD HETERODIMER OF THE CHROMATIN ACCESSIBILITY COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BYM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 2BYM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Cd Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BYM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nucleosome sliding]] | [[Category: nucleosome sliding]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:03:20 2007'' |
Revision as of 16:53, 18 December 2007
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HISTONE FOLD HETERODIMER OF THE CHROMATIN ACCESSIBILITY COMPLEX
Overview
The chromatin accessibility complex (CHRAC) is an abundant, evolutionarily, conserved nucleosome remodeling machinery able to catalyze histone octamer, sliding on DNA. CHRAC differs from the related ACF complex by the presence, of two subunits with molecular masses of 14 and 16 kDa, whose structure, and function were not known. We determined the structure of Drosophila, melanogaster CHRAC14-CHRAC16 by X-ray crystallography at 2.4-angstroms, resolution and found that they dimerize via a variant histone fold in a, typical handshake structure. In further analogy to histones, CHRAC14-16, contain unstructured N- and C-terminal tail domains that protrude from the, handshake structure. A dimer of CHRAC14-16 can associate with the N, terminus of ACF1, thereby completing CHRAC. Low-affinity interactions of, CHRAC14-16 with DNA significantly improve the efficiency of nucleosome, mobilization by limiting amounts of ACF. Deletion of the negatively, charged C terminus of CHRAC16 enhances DNA binding 25-fold but leads to, inhibition of nucleosome sliding, in striking analogy to the effect of the, DNA chaperone HMGB1 on nucleosome sliding. The presence of a surface, compatible with DNA interaction and the geometry of an H2A-H2B heterodimer, may provide a transient acceptor site for DNA dislocated from the histone, surface and therefore facilitate the nucleosome remodeling process.
About this Structure
2BYM is a Protein complex structure of sequences from Drosophila melanogaster with CD as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions., Hartlepp KF, Fernandez-Tornero C, Eberharter A, Grune T, Muller CW, Becker PB, Mol Cell Biol. 2005 Nov;25(22):9886-96. PMID:16260604
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