 |
PDBsum entry 5klh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Membrane protein
|
PDB id
|
|
|
|
5klh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural characterization reveals a novel bilobed architecture for the ectodomains of insect stage expressed trypanosoma brucei pssa-2 and trypanosoma congolense isa.
|
|
|
Authors
|
|
R.Ramaswamy,
S.Goomeshi nobary,
B.A.Eyford,
T.W.Pearson,
M.J.Boulanger.
|
|
|
Ref.
|
|
Protein Sci, 2016,
25,
2297-2302.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
African trypanosomiasis, caused by parasites of the genus Trypanosoma, is a
complex of devastating vector-borne diseases of humans and livestock in
sub-Saharan Africa. Central to the pathogenesis of African trypanosomes is their
transmission by the arthropod vector, Glossina spp. (tsetse fly). Intriguingly,
the efficiency of parasite transmission through the vector is reduced following
depletion of Trypanosoma brucei Procyclic-Specific Surface Antigen-2 (TbPSSA-2).
To investigate the underlying molecular mechanism of TbPSSA-2, we determined the
crystal structures of its ectodomain and that of its homolog T. congolense
Insect Stage Antigen (TcISA) to resolutions of 1.65 Å and 2.45 Å, respectively
using single wavelength anomalous dispersion. Both proteins adopt a novel
bilobed architecture with the individual lobes displaying rotational flexibility
around the central tether that suggest a potential mechanism for coordinating a
binding partner. In support of this hypothesis, electron density consistent with
a bound peptide was observed in the inter-lob cleft of a TcISA monomer. These
first reported structures of insect stage transmembrane proteins expressed by
African trypanosomes provide potentially valuable insight into the interface
between parasite and tsetse vector.
|
|
|
|
|
|
|
