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MALARIA PARASITE TRANSLOCON STRUCTURE AND MECHANISM OF EFFECTOR EXPORT

2018

Ho, Chi-Min;
Beck, Josh;
Lai, Mason;
Cui, Yanxiang;
Goldberg, Daniel;
Egea, Pascal;
Zhou, Z
et al.

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Malaria parasite translocon structure and mechanism of effector export\r
Architecture of the PTEX core complex\r
EXP2 forms a protein-conducting channel across PVM\r
PTEX150 forms an adaptor between HSP101 and EXP2\r
Endogenous cargo is observed in the channel of HSP101\r
Key interactions for PTEX assembly and function\r
Two observed states suggest a translocation mechanism\r
Discussion\r
Online content\r
Acknowledgements
Reviewer information
Fig. 1 Global architecture of the PTEX core complex in two cargo-bound states.
Fig. 2 EXP2 forms a heptameric pseudo-symmetric PVM-spanning pore.
Fig. 3 PTEX150 forms a heptameric flange-shaped adaptor between EXP2 and HSP101.
Fig. 4 Endogenous cargo bound in the channel of the HSP101 hexamer.
Fig. 5 Interactions essential for PTEX function.
Fig. 6 Mechanism of translocation.
Extended Data Fig. 1 Generation of HSP101–3×Flag P.
Extended Data Fig. 2 Detailed views of the PTEX protein-conducting channel and symmetry mismatch in the engaged state.
Extended Data Fig. 3 Detailed comparisons of the engaged and resetting states.
Extended Data Fig. 4 Resolution assessments of the two PTEX states.
Extended Data Fig. 5 Representative regions of cryo-EM density and atomic models.
Extended Data Fig. 6 Experimentally determined secondary structure elements and detected mass-spectrometry fragments mapped to the primary sequences of the three PTEX proteins.
Extended Data Fig. 7 Electron microscopy of the PTEX core complex.
Extended Data Fig. 8 Detergent belt, amino-terminal domain, and claw densities visible in maps at lower thresholds.
Extended Data Fig. 9 Data processing workflow.
Extended Data Table 1 Cryo-EM data collection, refinement and validation statistics.

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