2JSS

NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B

Summary for 2JSS

• Entry DOI: 10.2210/pdb2jss/pdb
• Related: 1YFQ
• NMR Information: BMRB: 15393
• Descriptor: Chimera of Histone H2B.1 and Histone H2A.Z, Uncharacterized protein YER030W (2 entities in total)
• Functional Keywords: histone-chaperone complex, intrinsically unfolded protein, chaperone-structural protein complex, chaperone-nuclear protein complex, chaperone/nuclear protein
• Biological source: Saccharomyces cerevisiae (yeast); More
• Cellular location: Nucleus: Q12692 P40019
• Total number of polymer chains: 2
• Total formula weight: 28033.68

Authors

Zhou, Z.,Feng, H.,Hansen, D.F.,Kato, H.,Luk, E.,Freedberg, D.I.,Kay, L.E.,Wu, C.,Bai, Y. (deposition date: 2007-07-11, release date: 2008-05-20, Last modification date: 2024-05-29)

Primary citation

Zhou, Z.,Feng, H.,Hansen, D.F.,Kato, H.,Luk, E.,Freedberg, D.I.,Kay, L.E.,Wu, C.,Bai, Y.
NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B.
Nat.Struct.Mol.Biol., 15:868-869, 2008

PubMed Abstract: The NMR structure of budding yeast chaperone Chz1 complexed with histones H2A.Z-H2B has been determined. Chz1 forms a long irregular chain capped by two short alpha-helices, and uses both positively and negatively charged residues to stabilize the histone dimer. A molecular model that docks Chz1 onto the nucleosome has implications for its potential functions.

PubMed: 18641662
DOI: 10.1038/nsmb.1465

Experimental method

SOLUTION NMR