6J2Z
AtFKBP53 N-terminal Nucleoplasmin Domain
Summary for 6J2Z
| Entry DOI | 10.2210/pdb6j2z/pdb |
| Related | 6J2M |
| Descriptor | Peptidyl-prolyl cis-trans isomerase FKBP53 (2 entities in total) |
| Functional Keywords | fkbp, fkbp-nucleoplasmin, histone chaperone, chaperone |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 10 |
| Total formula weight | 121116.09 |
| Authors | Singh, A.K.,Vasudevan, D. (deposition date: 2019-01-03, release date: 2019-12-04, Last modification date: 2023-11-22) |
| Primary citation | Singh, A.K.,Datta, A.,Jobichen, C.,Luan, S.,Vasudevan, D. AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains. Nucleic Acids Res., 48:1531-1550, 2020 Cited by PubMed Abstract: FKBP53 is one of the seven multi-domain FK506-binding proteins present in Arabidopsis thaliana, and it is known to get targeted to the nucleus. It has a conserved PPIase domain at the C-terminus and a highly charged N-terminal stretch, which has been reported to bind to histone H3 and perform the function of a histone chaperone. To better understand the molecular details of this PPIase with histone chaperoning activity, we have solved the crystal structures of its terminal domains and functionally characterized them. The C-terminal domain showed strong PPIase activity, no role in histone chaperoning and revealed a monomeric five-beta palm-like fold that wrapped over a helix, typical of an FK506-binding domain. The N-terminal domain had a pentameric nucleoplasmin-fold; making this the first report of a plant nucleoplasmin structure. Further characterization revealed the N-terminal nucleoplasmin domain to interact with H2A/H2B and H3/H4 histone oligomers, individually, as well as simultaneously, suggesting two different binding sites for H2A/H2B and H3/H4. The pentameric domain assists nucleosome assembly and forms a discrete complex with pre-formed nucleosomes; wherein two pentamers bind to a nucleosome. PubMed: 31807785DOI: 10.1093/nar/gkz1153 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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