PDBsum entry 5mlv

Motor protein

PDB id: 5mlv

Contents

Protein chains

(+ 0 more) 429 a.a.

(+ 0 more) 344 a.a.

(+ 0 more) 430 a.a.

Ligands

GTP ×6

ANP ×6

GDP ×6

EPB ×6

Metals

_MG ×6

PDB id:

5mlv

Name:

Motor protein

Title:

S. Pombe microtubule decorated with cut7 motor domain in the amppnp state

Structure:

Tubulin alpha-1 chain. Chain: e, m, b, h, k, q. Engineered: yes. Kinesin-like protein cut7. Chain: g, o, a, d, j, p. Synonym: cell untimely torn protein 7. Engineered: yes. Tubulin beta chain. Chain: i, n, c, f, l, r.

Source:

Schizosaccharomyces pombe 972h-. Fission yeast. Organism_taxid: 284812. Gene: nda2, spbc16a3.15c. Expressed in: schizosaccharomyces pombe. Expression_system_taxid: 4896. Gene: cut7, spac25g10.07c. Expressed in: escherichia coli. Expression_system_taxid: 562.

Authors:

C.A.Moores,O.Von Loeffelholz

Key ref:

O.von Loeffelholz et al. (2019). Cryo-EM Structure (4.5-Å) of Yeast Kinesin-5-Microtubule Complex Reveals a Distinct Binding Footprint and Mechanism of Drug Resistance. J Mol Biol, 431, 864-872. PubMed id: 30659798 DOI: 10.1016/j.jmb.2019.01.011

Date:

07-Dec-16 Release date: 08-Aug-18

Protein chains

P04688  (TBA1_SCHPO) -  Tubulin alpha-1 chain from Schizosaccharomyces pombe (strain 972 / ATCC 24843)

Seq: 455 a.a.

Struc: 429 a.a.

Protein chains

P24339  (CUT7_SCHPO) -  Kinesin-like protein cut7 from Schizosaccharomyces pombe (strain 972 / ATCC 24843)

Seq: 1085 a.a.

Struc: 344 a.a.

Protein chains

P05219  (TBB_SCHPO) -  Tubulin beta chain from Schizosaccharomyces pombe (strain 972 / ATCC 24843)

Seq: 448 a.a.

Struc: 430 a.a.

DOI no: 10.1016/j.jmb.2019.01.011

J Mol Biol 431:864-872 (2019)

PubMed id: 30659798

Cryo-EM Structure (4.5-Å) of Yeast Kinesin-5-Microtubule Complex Reveals a Distinct Binding Footprint and Mechanism of Drug Resistance.

O.von Loeffelholz, A.Peña, D.R.Drummond, R.Cross, C.A.Moores.

ABSTRACT

Kinesin-5s are microtubule-dependent motors that drive spindle pole separation during mitosis. We used cryo-electron microscopy to determine the 4.5-Å resolution structure of the motor domain of the fission yeast kinesin-5 Cut7 bound to fission yeast microtubules and explored the topology of the motor-microtubule interface and the susceptibility of the complex to drug binding. Despite their non-canonical architecture and mechanochemistry, Schizosaccharomyces pombe microtubules were stabilized by epothilone at the taxane binding pocket. The overall Cut7 footprint on the S. pombe microtubule surface is altered compared to mammalian tubulin microtubules because of their different polymer architectures. However, the core motor-microtubule interaction is tightly conserved, reflected in similar Cut7 ATPase activities on each microtubule type. AMPPNP-bound Cut7 adopts a kinesin-conserved ATP-like conformation including cover neck bundle formation. However, the Cut7 ATPase is not blocked by a mammalian-specific kinesin-5 inhibitor, consistent with the non-conserved sequence and structure of its loop5 insertion.