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6N2G

Crystal structure of Caenorhabditis elegans NAP1

Summary for 6N2G
Entry DOI10.2210/pdb6n2g/pdb
DescriptorNucleosome Assembly Protein (1 entity in total)
Functional Keywordsnucleosome assembly, histone binding, chaperone
Biological sourceCaenorhabditis elegans
Total number of polymer chains4
Total formula weight142826.84
Authors
Bhattacharyya, S.,DArcy, S. (deposition date: 2018-11-13, release date: 2019-01-30, Last modification date: 2024-03-13)
Primary citationSarkar, P.,Zhang, N.,Bhattacharyya, S.,Salvador, K.,D'Arcy, S.
Characterization of Caenorhabditis elegans Nucleosome Assembly Protein 1 Uncovers the Role of Acidic Tails in Histone Binding.
Biochemistry, 58:108-113, 2019
Cited by
PubMed Abstract: Nucleosome assembly proteins (Naps) influence chromatin dynamics by directly binding to histones. Here we provide a comprehensive structural and biochemical analysis of a Nap protein from Caenorhabditis elegans (CeNap1). CeNap1 naturally lacks the acidic N-terminal tail and has a short C-terminal tail compared to many other Nap proteins. Comparison of CeNap1 with full length and tail-less constructs of Saccharomyces cerevisiae Nap1 uncovers the role of these tails in self-association, histone binding, and Nap competition with DNA for H2A-H2B. We find that the presence of tails influences the stoichiometry of H2A-H2B binding and is required to complete the interactions between H2A-H2B and DNA. The absolute stoichiometry of the Nap protein and H2A-H2B complex is 2:1 or 2:2, with only a very small population of higher-order oligomers occurring at 150 mM NaCl. We also show that H3-H4 binds differently than H2A-H2B and that an (H3-H4) tetramer can simultaneously bind two Nap protein homodimers.
PubMed: 30521320
DOI: 10.1021/acs.biochem.8b01033
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.003 Å)
Structure validation

238895

数据于2025-07-16公开中

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