5X7V
Crystal structure of Nucleosome assembly protein S (PfNapS) from Plasmodium falciparum
Replaces: 3KYPSummary for 5X7V
| Entry DOI | 10.2210/pdb5x7v/pdb |
| Descriptor | Nucleosome assembly protein (1 entity in total) |
| Functional Keywords | nucleosome assembly protein, histone recognition, chaperone |
| Biological source | Plasmodium falciparum |
| Total number of polymer chains | 6 |
| Total formula weight | 137958.58 |
| Authors | Gill, J.,Yogavel, M.,Sharma, A. (deposition date: 2017-02-27, release date: 2017-03-15, Last modification date: 2024-03-27) |
| Primary citation | Gill, 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: 20377878DOI: 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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