The indicated residue numbering is based on hFKBP12, and secondary structures are based on AtFKBP53 CTD. ( A) Multiple sequence alignment of AtFKBP53 FKBD with human FKBP12 (HsFKBP12 UniProtKB – P62942), human FKBP13 (HsFKBP13 UniProtKB – P26885) and Burkholderia pseudomallei FKBP (BpFKBP UniProtKB – Q63J95) was done using the T-Coffee program. Sequence alignment and crystal structure of AtFKBP53 CTD reveals a canonical FKBD fold. Published by Oxford University Press on behalf of Nucleic Acids Research. The pentameric domain assists nucleosome assembly and forms a discrete complex with pre-formed nucleosomes wherein two pentamers bind to a nucleosome. 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 N-terminal domain had a pentameric nucleoplasmin-fold making this the first report of a plant nucleoplasmin structure. 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. 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. 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. 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.
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