6ZBG
Merozoite surface protein 1 (MSP-1) from Plasmodium falciparum, alternative conformation 4
Summary for 6ZBG
| Entry DOI | 10.2210/pdb6zbg/pdb |
| Related | 6ZBC 6ZBD 6ZBE 6ZBF 6ZBH 6ZBJ 6ZBL |
| EMDB information | 11150 11151 11152 11153 11154 11155 11156 11157 |
| Descriptor | Merozoite surface antigens, Merozoite surface protein-1, Merozoite surface protein 1, ... (4 entities in total) |
| Functional Keywords | merozoite surface protein 1, malaria, plasmodium falciparum, msp-1, p190, gpi-anchored membrane protein, membrane protein |
| Biological source | Plasmodium falciparum More |
| Total number of polymer chains | 4 |
| Total formula weight | 191624.99 |
| Authors | Dijkman, P.M.,Kudryashev, M. (deposition date: 2020-06-08, release date: 2021-05-19, Last modification date: 2024-11-06) |
| Primary citation | Dijkman, P.M.,Marzluf, T.,Zhang, Y.,Chang, S.S.,Helm, D.,Lanzer, M.,Bujard, H.,Kudryashev, M. Structure of the merozoite surface protein 1 from Plasmodium falciparum . Sci Adv, 7:-, 2021 Cited by PubMed Abstract: The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading 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 proteins associated with membrane and cytoskeleton interactions. MSP-1 formed dimers through these domains in a concentration-dependent manner. Dimerization is affected by the presence of the erythrocyte cytoskeleton protein spectrin, which may compete for the dimerization interface. Our work provides structural insights into the possible mode of interaction of MSP-1 with erythrocytes and establishes a framework for future investigations into the role of MSP-1 in infection and immunity. PubMed: 34078606DOI: 10.1126/sciadv.abg0465 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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