Single-particle cryo-EM of the full-length merozoite surface protein 1 from Plasmodium falciparum
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ABSTRACT:
SUBMITTER: Mikhail Kudryashev
PROVIDER: EMPIAR-10437 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structure of the merozoite surface protein 1 from <i>Plasmodium falciparum</i>.
Dijkman Patricia M PM Marzluf Tanja T Zhang Yingyi Y Chang Shih-Ying Scott SS Helm Dominic D Lanzer Michael M Bujard Hermann H Kudryashev Mikhail M
Science advances 20210602 23
The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading <i>Plasmodium</i> merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, entry into and escape from erythrocytes, and is a promising vaccine candidate. Here, we present monomeric and dimeric structures of full-length MSP-1. MSP-1 adopts an unusual fold with a large central cavity. Its fold includes several coiled-coils and shows structural homology to pr ...[more]
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