2AYU

The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling

2AYU の概要

• エントリーDOI: 10.2210/pdb2ayu/pdb
• 分子名称: Nucleosome assembly protein (1 entity in total)
• 機能のキーワード: nucleosome assembly protein 1 (nap1), histone chaperone, chaperone
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P25293
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47930.38

構造登録者

Park, Y.J.,Luger, K. (登録日: 2005-09-08, 公開日: 2006-02-07, 最終更新日: 2024-11-13)

主引用文献

Park, Y.J.,Luger, K.
The structure of nucleosome assembly protein 1.
Proc.Natl.Acad.Sci.Usa, 103:1248-1253, 2006

PubMed Abstract: Nucleosome assembly protein 1 (NAP-1) is an integral component in the establishment, maintenance, and dynamics of eukaryotic chromatin. It shuttles histones into the nucleus, assembles nucleosomes, and promotes chromatin fluidity, thereby affecting the transcription of many genes. The 3.0 A crystal structure of yeast NAP-1 reveals a previously uncharacterized fold with implications for histone binding and shuttling. A long alpha-helix is responsible for homodimerization via a previously uncharacterized antiparallel non-coiled-coil, and an alpha/beta domain is implicated in protein-protein interaction. A nuclear export sequence that is embedded in the dimerization helix is almost completely masked by an accessory domain that contains several target sites for casein kinase II. The four-stranded antiparallel beta-sheet that characterizes the alpha/beta domain is found in all histone chaperones, despite the absence of homology in sequence, structural context, or quaternary structure. To our knowledge, this is the first structure of a member of the large NAP family of proteins and suggests a mechanism by which the shuttling of histones to and from the nucleus is regulated.

PubMed: 16432217
DOI: 10.1073/pnas.0508002103

実験手法

X-RAY DIFFRACTION (3 Å)