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6GEN

Chromatin remodeller-nucleosome complex at 4.5 A resolution.

Summary for 6GEN
Entry DOI10.2210/pdb6gen/pdb
Related6GEJ
EMDB information4395 4396
DescriptorVacuolar protein sorting-associated protein 72, Vacuolar protein sorting-associated protein 71, RuvB-like protein 1, ... (16 entities in total)
Functional Keywordschromatin, remodeller, atpase, histone, nuclear protein
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Total number of polymer chains20
Total formula weight795586.86
Authors
Willhoft, O.,Chua, E.Y.D.,Wilkinson, M.,Wigley, D.B. (deposition date: 2018-04-27, release date: 2018-10-17, Last modification date: 2024-05-15)
Primary citationWillhoft, O.,Ghoneim, M.,Lin, C.L.,Chua, E.Y.D.,Wilkinson, M.,Chaban, Y.,Ayala, R.,McCormack, E.A.,Ocloo, L.,Rueda, D.S.,Wigley, D.B.
Structure and dynamics of the yeast SWR1-nucleosome complex.
Science, 362:-, 2018
Cited by
PubMed Abstract: The yeast SWR1 complex exchanges histone H2A in nucleosomes with Htz1 (H2A.Z in humans). The cryo-electron microscopy structure of the SWR1 complex bound to a nucleosome at 3.6-angstrom resolution reveals details of the intricate interactions between components of the SWR1 complex and its nucleosome substrate. Interactions between the Swr1 motor domains and the DNA wrap at superhelical location 2 distort the DNA, causing a bulge with concomitant translocation of the DNA by one base pair, coupled to conformational changes of the histone core. Furthermore, partial unwrapping of the DNA from the histone core takes place upon binding of nucleosomes to SWR1 complex. The unwrapping, as monitored by single-molecule data, is stabilized and has its dynamics altered by adenosine triphosphate binding but does not require hydrolysis.
PubMed: 30309918
DOI: 10.1126/science.aat7716
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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