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7Y5U

Cryo-EM structure of the monomeric human CAF1LC-H3-H4 complex

Summary for 7Y5U
Entry DOI10.2210/pdb7y5u/pdb
EMDB information33625
DescriptorChromatin assembly factor 1 subunit A, Histone H3.1, Histone H4, ... (5 entities in total)
Functional Keywordshistone chaperone, chromatin assembly factor, replication
Biological sourceHomo sapiens (human)
More
Total number of polymer chains5
Total formula weight168484.91
Authors
Liu, C.P.,Yu, Z.Y.,Yu, C.,Xu, R.M. (deposition date: 2022-06-17, release date: 2023-08-16, Last modification date: 2023-09-06)
Primary citationLiu, C.P.,Yu, Z.,Xiong, J.,Hu, J.,Song, A.,Ding, D.,Yu, C.,Yang, N.,Wang, M.,Yu, J.,Hou, P.,Zeng, K.,Li, Z.,Zhang, Z.,Zhang, X.,Li, W.,Zhang, Z.,Zhu, B.,Li, G.,Xu, R.M.
Structural insights into histone binding and nucleosome assembly by chromatin assembly factor-1.
Science, 381:eadd8673-eadd8673, 2023
Cited by
PubMed Abstract: Chromatin inheritance entails de novo nucleosome assembly after DNA replication by chromatin assembly factor-1 (CAF-1). Yet direct knowledge about CAF-1's histone binding mode and nucleosome assembly process is lacking. In this work, we report the crystal structure of human CAF-1 in the absence of histones and the cryo-electron microscopy structure of CAF-1 in complex with histones H3 and H4. One histone H3-H4 heterodimer is bound by one CAF-1 complex mainly through the p60 subunit and the acidic domain of the p150 subunit. We also observed a dimeric CAF-1-H3-H4 supercomplex in which two H3-H4 heterodimers are poised for tetramer assembly and discovered that CAF-1 facilitates right-handed DNA wrapping of H3-H4 tetramers. These findings signify the involvement of DNA in H3-H4 tetramer formation and suggest a right-handed nucleosome precursor in chromatin replication.
PubMed: 37616371
DOI: 10.1126/science.add8673
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

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