5M4T

C-terminal domain structure of VSG M1.1

Summary for 5M4T

• Entry DOI: 10.2210/pdb5m4t/pdb
• NMR Information: BMRB: 34055
• Descriptor: Variant surface glycoprotein MITAT 1.1 (1 entity in total)
• Functional Keywords: variant surface glycoprotein immune evasion trypanosoma brucei gpi-anchored protein, membrane protein
• Biological source: Trypanosoma brucei brucei
• Total number of polymer chains: 1
• Total formula weight: 8156.06

Authors

Jones, N.G.,Mott, H.R.,Carrington, M. (deposition date: 2016-10-19, release date: 2017-09-20, Last modification date: 2024-10-23)

Primary citation

Bartossek, T.,Jones, N.G.,Schafer, C.,Cvitkovic, M.,Glogger, M.,Mott, H.R.,Kuper, J.,Brennich, M.,Carrington, M.,Smith, A.S.,Fenz, S.,Kisker, C.,Engstler, M.
Structural basis for the shielding function of the dynamic trypanosome variant surface glycoprotein coat.
Nat Microbiol, 2:1523-1532, 2017

PubMed Abstract: The most prominent defence of the unicellular parasite Trypanosoma brucei against the host immune system is a dense coat that comprises a variant surface glycoprotein (VSG). Despite the importance of the VSG family, no complete structure of a VSG has been reported. Making use of high-resolution structures of individual VSG domains, we employed small-angle X-ray scattering to elucidate the first two complete VSG structures. The resulting models imply that the linker regions confer great flexibility between domains, which suggests that VSGs can adopt two main conformations to respond to obstacles and changes of protein density, while maintaining a protective barrier at all times. Single-molecule diffusion measurements of VSG in supported lipid bilayers substantiate this possibility, as two freely diffusing populations could be detected. This translates into a highly flexible overall topology of the surface VSG coat, which displays both lateral movement in the plane of the membrane and variation in the overall thickness of the coat.

PubMed: 28894098
DOI: 10.1038/s41564-017-0013-6

Experimental method

SOLUTION NMR