5MJS
S. pombe microtubule copolymerized with GTP and Mal3-143
Summary for 5MJS
| Entry DOI | 10.2210/pdb5mjs/pdb |
| EMDB information | 3522 |
| Descriptor | Tubulin beta chain, Microtubule integrity protein mal3, Tubulin alpha-1 chain, ... (5 entities in total) |
| Functional Keywords | schizosaccharomyces pombe microtubules, structural protein |
| Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) More |
| Total number of polymer chains | 9 |
| Total formula weight | 408553.88 |
| Authors | von Loeffelholz, O.,Moores, C. (deposition date: 2016-12-01, release date: 2017-12-20, Last modification date: 2019-10-23) |
| Primary citation | von Loeffelholz, O.,Venables, N.A.,Drummond, D.R.,Katsuki, M.,Cross, R.,Moores, C.A. Nucleotide- and Mal3-dependent changes in fission yeast microtubules suggest a structural plasticity view of dynamics. Nat Commun, 8:2110-2110, 2017 Cited by PubMed Abstract: Using cryo-electron microscopy, we characterize the architecture of microtubules assembled from Schizosaccharomyces pombe tubulin, in the presence and absence of their regulatory partner Mal3. Cryo-electron tomography reveals that microtubules assembled from S. pombe tubulin have predominantly B-lattice interprotofilament contacts, with protofilaments skewed around the microtubule axis. Copolymerization with Mal3 favors 13 protofilament microtubules with reduced protofilament skew, indicating that Mal3 adjusts interprotofilament interfaces. A 4.6-Å resolution structure of microtubule-bound Mal3 shows that Mal3 makes a distinctive footprint on the S. pombe microtubule lattice and that unlike mammalian microtubules, S. pombe microtubules do not show the longitudinal lattice compaction associated with EB protein binding and GTP hydrolysis. Our results firmly support a structural plasticity view of microtubule dynamics in which microtubule lattice conformation is sensitive to a variety of effectors and differently so for different tubulins. PubMed: 29235477DOI: 10.1038/s41467-017-02241-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.6 Å) |
Structure validation
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