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5X7V

Crystal structure of Nucleosome assembly protein S (PfNapS) from Plasmodium falciparum

Replaces:  3KYP
Summary for 5X7V
Entry DOI10.2210/pdb5x7v/pdb
DescriptorNucleosome assembly protein (1 entity in total)
Functional Keywordsnucleosome assembly protein, histone recognition, chaperone
Biological sourcePlasmodium falciparum
Total number of polymer chains6
Total formula weight137958.58
Authors
Gill, J.,Yogavel, M.,Sharma, A. (deposition date: 2017-02-27, release date: 2017-03-15, Last modification date: 2024-03-27)
Primary citationGill, J.,Kumar, A.,Yogavel, M.,Belrhali, H.,Jain, S.K.,Rug, M.,Brown, M.,Maier, A.G.,Sharma, A.
Structure, localization and histone binding properties of nuclear-associated nucleosome assembly protein from Plasmodium falciparum.
Malar. J., 9:90-90, 2010
Cited by
PubMed Abstract: Nucleosome assembly proteins (NAPs) are histone chaperones that are crucial for the shuttling and incorporation of histones into nucleosomes. NAPs participate in the assembly and disassembly of nucleosomes thus contributing to chromatin structure organization. The human malaria parasite Plasmodium falciparum contains two nucleosome assembly proteins termed PfNapL and PfNapS.
PubMed: 20377878
DOI: 10.1186/1475-2875-9-90
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.802 Å)
Structure validation

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