6E0C
Cryo-EM structure of the CENP-A nucleosome (W601) in complex with a single chain antibody fragment
Summary for 6E0C
Entry DOI | 10.2210/pdb6e0c/pdb |
EMDB information | 8938 8945 8949 |
Descriptor | Histone H3-like centromeric protein A, Histone H4, Histone H2A type 1-B/E, ... (7 entities in total) |
Functional Keywords | cenp-a, centromere, widom's 601 dna, anti-nucleosome antibody, acidic patch, nuclear protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 12 |
Total formula weight | 263877.17 |
Authors | Yadav, K.N.S.,Zhou, B.-R. (deposition date: 2018-07-06, release date: 2019-05-22, Last modification date: 2024-10-23) |
Primary citation | Zhou, B.R.,Yadav, K.N.S.,Borgnia, M.,Hong, J.,Cao, B.,Olins, A.L.,Olins, D.E.,Bai, Y.,Zhang, P. Atomic resolution cryo-EM structure of a native-like CENP-A nucleosome aided by an antibody fragment. Nat Commun, 10:2301-2301, 2019 Cited by PubMed Abstract: Genomic DNA in eukaryotes is organized into chromatin through association with core histones to form nucleosomes, each distinguished by their DNA sequences and histone variants. Here, we used a single-chain antibody fragment (scFv) derived from the anti-nucleosome antibody mAb PL2-6 to stabilize human CENP-A nucleosome containing a native α-satellite DNA and solved its structure by the cryo-electron microscopy (cryo-EM) to 2.6 Å resolution. In comparison, the corresponding cryo-EM structure of the free CENP-A nucleosome could only reach 3.4 Å resolution. We find that scFv binds to a conserved acidic patch on the histone H2A-H2B dimer without perturbing the nucleosome structure. Our results provide an atomic resolution cryo-EM structure of a nucleosome and insight into the structure and function of the CENP-A nucleosome. The scFv approach is applicable to the structural determination of other native-like nucleosomes with distinct DNA sequences. PubMed: 31127102DOI: 10.1038/s41467-019-10247-4 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.63 Å) |
Structure validation
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