9GXA
CENP-A/H4 di-tetrasome assembled on alpha-satellite DNA.
Summary for 9GXA
| Entry DOI | 10.2210/pdb9gxa/pdb |
| EMDB information | 51645 |
| Descriptor | Histone H3-like centromeric protein A, Histone H4, 147 bp human alpha-satellite DNA, ... (4 entities in total) |
| Functional Keywords | cenp-a/h4, di-tetrasome, nucleosome, centromere, cenp-a, human, cell division., dna binding protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 10 |
| Total formula weight | 199346.77 |
| Authors | |
| Primary citation | Ali-Ahmad, A.,Mors, M.,Carrer, M.,Li, X.,Bilokapic, S.,Halic, M.,Cascella, M.,Sekulic, N. Non-nucleosomal (CENP-A/H4) 2 - DNA complexes as a possible platform for centromere organization. Biorxiv, 2025 Cited by PubMed Abstract: The centromere is a part of the chromosome that is essential for the even segregation of duplicated chromosomes during cell division. It is epigenetically defined by the presence of the histone H3 variant CENP-A. CENP-A associates specifically with a group of 16 proteins that form the centromere-associated network of proteins (CCAN). In mitosis, the kinetochore forms on the CCAN to connect the duplicated chromosomes to the microtubules protruding from the cell poles. Previous studies have shown that CENP-A replaces H3 in nucleosomes, and recently the structures of CENP-A-containing nucleosomes in complex with CCANs have been revealed, but they show only a limited interaction between CCANs and CENP-A. Here, we report the cryoEM structure of 2x(CENP-A/H4)-di-tetramers assembled on DNA in the absence of H2A/H2B histone dimer and speculate how (CENP-A/H4)-tetramers and -di-tetramers might serve as a platform for CCAN organization. PubMed: 39803555DOI: 10.1101/2024.12.31.630874 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.01 Å) |
Structure validation
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