3R45

Structure of a CENP-A-Histone H4 Heterodimer in complex with chaperone HJURP

Summary for 3R45

• Entry DOI: 10.2210/pdb3r45/pdb
• Descriptor: Histone H3-like centromeric protein A, Histone H4, Holliday junction recognition protein, ... (6 entities in total)
• Functional Keywords: histone fold, centromere, cenp-a, histone chaperone, hjurp, nuclear protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P49450 P62805; Nucleus, nucleolus: Q8NCD3
• Total number of polymer chains: 3
• Total formula weight: 40400.03

Authors

Hu, H.,Liu, Y.,Wang, M.,Fang, J.,Huang, H.,Yang, N.,Li, Y.,Wang, J.,Yao, X.,Shi, Y.,Li, G.,Xu, R.M. (deposition date: 2011-03-17, release date: 2011-04-06, Last modification date: 2023-11-01)

Primary citation

Hu, H.,Liu, Y.,Wang, M.,Fang, J.,Huang, H.,Yang, N.,Li, Y.,Wang, J.,Yao, X.,Shi, Y.,Li, G.,Xu, R.M.
Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP
Genes Dev., 25:901-906, 2011

PubMed Abstract: In higher eukaryotes, the centromere is epigenetically specified by the histone H3 variant Centromere Protein-A (CENP-A). Deposition of CENP-A to the centromere requires histone chaperone HJURP (Holliday junction recognition protein). The crystal structure of an HJURP-CENP-A-histone H4 complex shows that HJURP binds a CENP-A-H4 heterodimer. The C-terminal β-sheet domain of HJURP caps the DNA-binding region of the histone heterodimer, preventing it from spontaneous association with DNA. Our analysis also revealed a novel site in CENP-A that distinguishes it from histone H3 in its ability to bind HJURP. These findings provide key information for specific recognition of CENP-A and mechanistic insights into the process of centromeric chromatin assembly.

PubMed: 21478274
DOI: 10.1101/gad.2045111

Experimental method

X-RAY DIFFRACTION (2.6 Å)