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5W3F

Yeast tubulin polymerized with GTP in vitro

Summary for 5W3F
Entry DOI10.2210/pdb5w3f/pdb
EMDB information8755 8756 8757 8758 8759
DescriptorTubulin alpha-1 chain, Tubulin beta chain, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordscytoskeleton, tubulin, hydrolase
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
More
Total number of polymer chains2
Total formula weight101812.01
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 citationHowes, 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: 28652389
DOI: 10.1083/jcb.201612195
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.7 Å)
Structure validation

237735

数据于2025-06-18公开中

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