5W3H
Yeast microtubule stabilized with epothilone
Summary for 5W3H
Entry DOI | 10.2210/pdb5w3h/pdb |
Related | 5W3F 5W3J |
EMDB information | 8755 8756 8757 8758 8759 |
Descriptor | Tubulin alpha-1 chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total) |
Functional Keywords | cytoskeleton, tubulin, hydrolase |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
Total number of polymer chains | 2 |
Total formula weight | 102305.67 |
Authors | Howes, S.C.,Geyer, E.A.,LaFrance, B.,Zhang, R.,Kellogg, E.H.,Westermann, S.,Rice, L.M.,Nogales, E. (deposition date: 2017-06-07, release date: 2017-07-19, Last modification date: 2024-03-13) |
Primary citation | Howes, S.C.,Geyer, E.A.,LaFrance, B.,Zhang, R.,Kellogg, E.H.,Westermann, S.,Rice, L.M.,Nogales, E. Structural differences between yeast and mammalian microtubules revealed by cryo-EM. J. Cell Biol., 216:2669-2677, 2017 Cited by PubMed Abstract: Microtubules are polymers of αβ-tubulin heterodimers essential for all eukaryotes. Despite sequence conservation, there are significant structural differences between microtubules assembled in vitro from mammalian or budding yeast tubulin. Yeast MTs were not observed to undergo compaction at the interdimer interface as seen for mammalian microtubules upon GTP hydrolysis. Lack of compaction might reflect slower GTP hydrolysis or a different degree of allosteric coupling in the lattice. The microtubule plus end-tracking protein Bim1 binds yeast microtubules both between αβ-tubulin heterodimers, as seen for other organisms, and within tubulin dimers, but binds mammalian tubulin only at interdimer contacts. At the concentrations used in cryo-electron microscopy, Bim1 causes the compaction of yeast microtubules and induces their rapid disassembly. Our studies demonstrate structural differences between yeast and mammalian microtubules that likely underlie their differing polymerization dynamics. These differences may reflect adaptations to the demands of different cell size or range of physiological growth temperatures. PubMed: 28652389DOI: 10.1083/jcb.201612195 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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