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PDBsum entry 5klh

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protein ligands Protein-protein interface(s) links
Membrane protein PDB id
5klh

 

 

 

 

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Contents
Protein chains
221 a.a.
Ligands
SO4
Waters ×462
PDB id:
5klh
Name: Membrane protein
Title: Crystal structure of trypanosoma brucei procyclic specific surface antigen-2
Structure: Surface glycoprotein. Chain: a, b. Fragment: residues 40-262. Engineered: yes
Source: Trypanosoma brucei. Organism_taxid: 5691. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.65Å     R-factor:   0.179     R-free:   0.214
Authors: R.Ramaswamy,M.L.Parker,M.J.Boulanger
Key ref: R.Ramaswamy et al. (2016). Structural characterization reveals a novel bilobed architecture for the ectodomains of insect stage expressed Trypanosoma brucei PSSA-2 and Trypanosoma congolense ISA. Protein Sci, 25, 2297-2302. PubMed id: 27671214
Date:
24-Jun-16     Release date:   05-Jul-17    
PROCHECK
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 Headers
 References

Protein chains
Q26806  (Q26806_9TRYP) -  Surface glycoprotein from Trypanosoma brucei
Seq:
Struc:
412 a.a.
221 a.a.*
Key:    Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
Protein Sci 25:2297-2302 (2016)
PubMed id: 27671214  
 
 
Structural characterization reveals a novel bilobed architecture for the ectodomains of insect stage expressed Trypanosoma brucei PSSA-2 and Trypanosoma congolense ISA.
R.Ramaswamy, S.Goomeshi Nobary, B.A.Eyford, T.W.Pearson, M.J.Boulanger.
 
  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.
 

 

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