7MIZ
Atomic structure of cortical microtubule from Toxoplasma gondii
This is a non-PDB format compatible entry.
Summary for 7MIZ
| Entry DOI | 10.2210/pdb7miz/pdb |
| EMDB information | 23869 23870 |
| Descriptor | Microtubule associated protein SPM1, Tubulin alpha chain, Tubulin beta chain, ... (8 entities in total) |
| Functional Keywords | cortical, parasite, structural protein |
| Biological source | Toxoplasma gondii More |
| Total number of polymer chains | 100 |
| Total formula weight | 4151024.13 |
| Authors | Wang, X.,Brown, A.,Sibley, L.D.,Zhang, R. (deposition date: 2021-04-18, release date: 2021-06-02, Last modification date: 2024-10-23) |
| Primary citation | Wang, X.,Fu, Y.,Beatty, W.L.,Ma, M.,Brown, A.,David Sibley, L.,Zhang, R. Cryo-EM structure of cortical microtubules from human parasite Toxoplasma gondii identifies their microtubule inner proteins. Nat Commun, 12:3065-3065, 2021 Cited by PubMed Abstract: In living cells, microtubules (MTs) play pleiotropic roles, which require very different mechanical properties. Unlike the dynamic MTs found in the cytoplasm of metazoan cells, the specialized cortical MTs from Toxoplasma gondii, a prevalent human pathogen, are extraordinarily stable and resistant to detergent and cold treatments. Using single-particle cryo-EM, we determine their ex vivo structure and identify three proteins (TrxL1, TrxL2 and SPM1) as bona fide microtubule inner proteins (MIPs). These three MIPs form a mesh on the luminal surface and simultaneously stabilize the tubulin lattice in both longitudinal and lateral directions. Consistent with previous observations, deletion of the identified MIPs compromises MT stability and integrity under challenges by chemical treatments. We also visualize a small molecule like density at the Taxol-binding site of β-tubulin. Our results provide the structural basis to understand the stability of cortical MTs and suggest an evolutionarily conserved mechanism of MT stabilization from the inside. PubMed: 34031406DOI: 10.1038/s41467-021-23351-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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