8TXC
Characterization of the Chlamydomonas Flagellar Mastigoneme Filament Subunit MST1 Structure at 3.9 angstrom
Summary for 8TXC
| Entry DOI | 10.2210/pdb8txc/pdb |
| Related | 8XTC |
| EMDB information | 41679 41680 |
| Descriptor | Mastigoneme-like protein (1 entity in total) |
| Functional Keywords | fibrous flagellar hairs, structural protein |
| Biological source | Chlamydomonas reinhardtii |
| Total number of polymer chains | 1 |
| Total formula weight | 205404.20 |
| Authors | |
| Primary citation | Wang, Y.,Yang, J.,Hu, F.,Yang, Y.,Huang, K.,Zhang, K. Cryo-EM reveals how the mastigoneme assembles and responds to environmental signal changes. J.Cell Biol., 222:-, 2023 Cited by PubMed Abstract: Mastigonemes are thread-like structures adorning the flagella of protists. In Chlamydomonas reinhardtii, filamentous mastigonemes find their roots in the flagella's distal region, associated with the channel protein PKD2, implying their potential contribution to external signal sensing and flagellar motility control. Here, we present the single-particle cryo-electron microscopy structure of the mastigoneme at 3.4 Å. The filament unit, MST1, consists of nine immunoglobulin-like domains and six Sushi domains, trailed by an elastic polyproline-II helix. Our structure demonstrates that MST1 subunits are periodically assembled to form a centrosymmetric, non-polar filament. Intriguingly, numerous clustered disulfide bonds within a ladder-like spiral configuration underscore structural resilience. While defects in the mastigoneme structure did not noticeably affect general attributes of cell swimming, they did impact specific swimming properties, particularly under varied environmental conditions such as redox shifts and heightened viscosity. Our findings illuminate the potential role of mastigonemes in flagellar motility and suggest their involvement in diverse environmental responses. PubMed: 37882754DOI: 10.1083/jcb.202301066 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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