2Z2R

Nucleosome assembly proteins I (NAP-1, 74-365)

Summary for 2Z2R

• Entry DOI: 10.2210/pdb2z2r/pdb
• Descriptor: Nucleosome assembly protein (1 entity in total)
• Functional Keywords: nucleosome assembly protein 1 (nap1), histone chaperone, chaperone
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P25293
• Total number of polymer chains: 2
• Total formula weight: 67759.62

Authors

Park, Y.J.,Luger, K. (deposition date: 2007-05-25, release date: 2008-03-11, Last modification date: 2024-10-30)

Primary citation

Park, Y.J.,McBryant, S.J.,Luger, K.
A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1
J.Mol.Biol., 375:1076-1085, 2008

PubMed Abstract: The histone chaperone nucleosome assembly protein 1 (NAP1) is implicated in histone shuttling as well as nucleosome assembly and disassembly. Under physiological conditions, NAP1 dimers exist in a mixture of various high-molecular-weight oligomers whose size may be regulated by the cell cycle-dependent concentration of NAP1. Both the functional and structural significance of the observed oligomers are unknown. We have resolved the molecular mechanism by which yeast NAP1 (yNAP1) dimers oligomerize by applying x-ray crystallographic, hydrodynamic, and functional approaches. We found that an extended beta-hairpin that protrudes from the compact core of the yNAP1 dimer forms a stable beta-sheet with beta-hairpins of neighboring yNAP1 dimers. Disruption of the beta-hairpin (whose sequence is conserved among NAP1 proteins in various species) by the replacement of one or more amino acids with proline results in complete loss of yNAP1 dimer oligomerization. The in vitro functions of yNAP1 remain unaffected by the mutations. We have thus identified a conserved structural feature of NAP1 whose function, in addition to presenting the nuclear localization sequence, appears to be the formation of higher-order oligomers.

PubMed: 18068721
DOI: 10.1016/j.jmb.2007.11.031

Experimental method

X-RAY DIFFRACTION (3.2 Å)