2FJ7

Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element

Summary for 2FJ7

• Entry DOI: 10.2210/pdb2fj7/pdb
• Related: 1AOI 1KX5
• Descriptor: 147 bp DNA containing 16 bp poly dA element, 147 bp DNA containing 16 bp poly dT element, histone H3, ... (6 entities in total)
• Functional Keywords: protein-dna complex, narrow minor groove, structural protein-dna complex, structural protein/dna
• Biological source: Xenopus laevis (African clawed frog); More
• Cellular location: Nucleus: P62799 P02281
• Total number of polymer chains: 10
• Total formula weight: 199506.17

Authors

Bao, Y.,White, C.L.,Luger, K. (deposition date: 2005-12-31, release date: 2006-09-26, Last modification date: 2024-02-14)

Primary citation

Bao, Y.,White, C.L.,Luger, K.
Nucleosome Core Particles Containing a Poly(dA.dT) Sequence Element Exhibit a Locally Distorted DNA Structure.
J.Mol.Biol., 361:617-624, 2006

PubMed Abstract: Poly(dA.dT) DNA sequence elements are thought to promote transcription by either excluding nucleosomes or by altering their structural or dynamic properties. Here, the stability and structure of a defined nucleosome core particle containing a 16 base-pair poly(dA.dT) element (A16 NCP) was investigated. The A16 NCP requires a significantly higher temperature for histone octamer sliding in vitro compared to comparable nucleosomes that do not contain a poly(dA.dT) element. Fluorescence resonance energy transfer showed that the interactions between the nucleosomal DNA ends and the histone octamer were destabilized in A16 NCP. The crystal structure of A16 NCP was determined to a resolution of 3.2 A. The overall structure was maintained except for local deviations in DNA conformation. These results are consistent with previous in vivo and in vitro observations that poly(dA.dT) elements cause only modest changes in DNA accessibility and modest increases in steady-state transcription levels.

PubMed: 16860337
DOI: 10.1016/j.jmb.2006.06.051

Experimental method

X-RAY DIFFRACTION (3.2 Å)