6J2M

Crystal structure of AtFKBP53 C-terminal domain

6J2M の概要

• エントリーDOI: 10.2210/pdb6j2m/pdb
• 分子名称: Peptidyl-prolyl cis-trans isomerase FKBP53, 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: fkbp, ppiase, immunophilin, prolyl isomerase, chaperone, isomerase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14505.66

構造登録者

Singh, A.K.,Vasudevan, D. (登録日: 2019-01-01, 公開日: 2019-12-04, 最終更新日: 2023-11-22)

主引用文献

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

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: 31807785
DOI: 10.1093/nar/gkz1153

実験手法

X-RAY DIFFRACTION (1.13 Å)