PDBsum entry 5w3h

Hydrolase

PDB id: 5w3h

Contents

Protein chains

440 a.a.

427 a.a.

Ligands

GTP

GDP

_EP

Metals

_MG

PDB id:

5w3h

Name:

Hydrolase

Title:

Yeast microtubule stabilized with epothilone

Structure:

Tubulin alpha-1 chain. Chain: a. Tubulin beta chain. Chain: b. Synonym: beta-tubulin

Source:

Saccharomyces cerevisiae (strain atcc 204508 / s288c). Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Strain: atcc 204508 / s288c

Authors:

S.C.Howes,E.A.Geyer,B.Lafrance,R.Zhang,E.H.Kellogg,S.Westermann, L.M.Rice,E.Nogales

Key ref:

S.C.Howes et al. (2017). Structural differences between yeast and mammalian microtubules revealed by cryo-EM. J Cell Biol, 216, 2669-2677. PubMed id: 28652389

Date:

07-Jun-17 Release date: 19-Jul-17

Protein chain

P09733  (TBA1_YEAST) -  Tubulin alpha-1 chain from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 447 a.a.

Struc: 440 a.a.

Protein chain

P02557  (TBB_YEAST) -  Tubulin beta chain from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 457 a.a.

Struc: 428 a.a.

Enzyme reactions

• Enzyme class 1: Chain A: E.C.3.6.5.- - ?????
• Enzyme class 2: Chain B: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

J Cell Biol 216:2669-2677 (2017)

PubMed id: 28652389

Structural differences between yeast and mammalian microtubules revealed by cryo-EM.

S.C.Howes, E.A.Geyer, B.LaFrance, R.Zhang, E.H.Kellogg, S.Westermann, L.M.Rice, E.Nogales.

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.