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1aoi
From Proteopedia
| 1aoi, resolution 2.80Å () | |||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT
The X-ray crystal structure of the nucleosome core particle of chromatin shows in atomic detail how the histone protein octamer is assembled and how 146 base pairs of DNA are organized into a superhelix around it. Both histone/histone and histone/DNA interactions depend on the histone fold domains and additional, well ordered structure elements extending from this motif. Histone amino-terminal tails pass over and between the gyres of the DNA superhelix to contact neighbouring particles. The lack of uniformity between multiple histone/DNA-binding sites causes the DNA to deviate from ideal superhelix geometry.
Crystal structure of the nucleosome core particle at 2.8 A resolution., Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ, Nature. 1997 Sep 18;389(6648):251-60. PMID:9305837
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1AOI is a 10 chains structure of sequences from Xenopus laevis. The July 2000 RCSB PDB Molecule of the Month feature on Nucleosome by David S. Goodsell is 10.2210/rcsb_pdb/mom_2000_7. Full crystallographic information is available from OCA.
PDB ID 1AOI |
contains two copies of each histone protein (H2A, H2B, H3, H4) and 146 basepairs (bp) of superhelical DNA wrapped around this histone octamer. It represents the first order of DNA packaging in the nucleus and as such is the principal structure that determines DNA accessibility.
For a more detailed exploration of this structure, see Nucleosome Structure at the Online Macromolecular Museum.
Reference
- Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature. 1997 Sep 18;389(6648):251-60. PMID:9305837 doi:10.1038/38444
Page seeded by OCA on Wed Feb 18 02:45:37 2009
