2byk

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Revision as of 20:59, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2byk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2byk, resolution 2.40Å" /> '''HISTONE FOLD HETERO...)
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File:2byk.gif


2byk, resolution 2.40Å

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HISTONE FOLD HETERODIMER OF THE CHROMATIN ACCESSIBILITY COMPLEX

OverviewOverview

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 ... [(full description)]

About this StructureAbout this Structure

2BYK is a [Protein complex] structure of sequences from [Drosophila melanogaster] with SO4 as [ligand]. Full crystallographic information is available from [OCA].

ReferenceReference

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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