2N87

Solution structure of the PPIase domain of TbPar42

Replaces:  2MNT

Summary for 2N87

• Entry DOI: 10.2210/pdb2n87/pdb
• Related: 2N84
• NMR Information: BMRB: 19904
• Descriptor: Uncharacterized protein (1 entity in total)
• Functional Keywords: ppiase domain, parvulin, isomerase
• Biological source: Trypanosoma brucei brucei TREU927
• Total number of polymer chains: 1
• Total formula weight: 13522.22

Authors

Rehic, E.,Bayer, P. (deposition date: 2015-10-05, release date: 2016-10-12, Last modification date: 2024-05-15)

Primary citation

Rehic, E.,Hoenig, D.,Kamba, B.E.,Goehring, A.,Hofmann, E.,Gasper, R.,Matena, A.,Bayer, P.
Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei.
Biomolecules, 9:-, 2019

PubMed Abstract: is a unicellular eukaryotic parasite, which causes the African sleeping sickness in humans. The recently discovered trypanosomal protein Parvulin 42 (Par42) plays a key role in parasite cell proliferation. Homologues of this two-domain protein are exclusively found in protozoa species. Par42 exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl--isomerase (PPIase) domain, both connected by a linker. Using NMR and X-ray analysis as well as activity assays, we report on the structures of the single domains of Par42, discuss their intra-molecular interplay, and give some initial hints as to potential cellular functions of the protein.

PubMed: 30866577
DOI: 10.3390/biom9030093

Experimental method

SOLUTION NMR