6GMP

CRYSTAL STRUCTURE OF THE PPIASE DOMAIN OF TBPAR42

Summary for 6GMP

• Entry DOI: 10.2210/pdb6gmp/pdb
• Related: 2MNT 2N84 2N87
• Descriptor: PARVULIN 42 (2 entities in total)
• Functional Keywords: ppiase, isomerase
• Biological source: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
• Total number of polymer chains: 1
• Total formula weight: 13676.39

Authors

Hoenig, D.,Rute, A.,Hofmann, E.,Bayer, P.,Gasper, R. (deposition date: 2018-05-28, release date: 2019-03-20, Last modification date: 2024-05-01)

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 ofTrypanosoma 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

X-RAY DIFFRACTION (1.35 Å)