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Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei

Trypanosoma brucei is a unicellular eukaryotic parasite, which causes the African sleeping sickness in humans. The recently discovered trypanosomal protein Parvulin 42 (TbPar42) plays a key role in parasite cell proliferation. Homologues of this two-domain protein are exclusively found in protozoa s...

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Autores principales: Rehic, Edisa, Hoenig, Dana, Kamba, Bianca E., Goehring, Anna, Hofmann, Eckhard, Gasper, Raphael, Matena, Anja, Bayer, Peter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6468809/
https://www.ncbi.nlm.nih.gov/pubmed/30866577
http://dx.doi.org/10.3390/biom9030093
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author Rehic, Edisa
Hoenig, Dana
Kamba, Bianca E.
Goehring, Anna
Hofmann, Eckhard
Gasper, Raphael
Matena, Anja
Bayer, Peter
author_facet Rehic, Edisa
Hoenig, Dana
Kamba, Bianca E.
Goehring, Anna
Hofmann, Eckhard
Gasper, Raphael
Matena, Anja
Bayer, Peter
author_sort Rehic, Edisa
collection PubMed
description Trypanosoma brucei is a unicellular eukaryotic parasite, which causes the African sleeping sickness in humans. The recently discovered trypanosomal protein Parvulin 42 (TbPar42) plays a key role in parasite cell proliferation. Homologues of this two-domain protein are exclusively found in protozoa species. TbPar42 exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-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 TbPar42, discuss their intra-molecular interplay, and give some initial hints as to potential cellular functions of the protein.
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spelling pubmed-64688092019-04-24 Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei Rehic, Edisa Hoenig, Dana Kamba, Bianca E. Goehring, Anna Hofmann, Eckhard Gasper, Raphael Matena, Anja Bayer, Peter Biomolecules Article Trypanosoma brucei is a unicellular eukaryotic parasite, which causes the African sleeping sickness in humans. The recently discovered trypanosomal protein Parvulin 42 (TbPar42) plays a key role in parasite cell proliferation. Homologues of this two-domain protein are exclusively found in protozoa species. TbPar42 exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-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 TbPar42, discuss their intra-molecular interplay, and give some initial hints as to potential cellular functions of the protein. MDPI 2019-03-07 /pmc/articles/PMC6468809/ /pubmed/30866577 http://dx.doi.org/10.3390/biom9030093 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Rehic, Edisa
Hoenig, Dana
Kamba, Bianca E.
Goehring, Anna
Hofmann, Eckhard
Gasper, Raphael
Matena, Anja
Bayer, Peter
Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei
title Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei
title_full Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei
title_fullStr Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei
title_full_unstemmed Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei
title_short Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei
title_sort structural analysis of the 42 kda parvulin of trypanosoma brucei
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6468809/
https://www.ncbi.nlm.nih.gov/pubmed/30866577
http://dx.doi.org/10.3390/biom9030093
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