PDBsum entry 6b0c

Motor protein/structural protein

PDB id: 6b0c

Contents

Protein chains

439 a.a.

425 a.a.

336 a.a.

Ligands

GTP ×2

GDP ×2

TA1

ANP

Metals

_MG ×3

PDB id:

6b0c

Name:

Motor protein/structural protein

Title:

Klp10a-amppnp in complex with curved tubulin and a microtubule

Structure:

Tubulin alpha-1b chain. Chain: a, c. Synonym: alpha-tubulin ubiquitous, tubulin k-alpha-1, tubulin alpha- ubiquitous chain. Tubulin beta chain. Chain: b, d. Kinesin-like protein klp10a. Chain: k. Fragment: motor (unp residues 279-615).

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Organ: brain. Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: klp10a, cg1453. Expressed in: escherichia coli bl21(de3).

Authors:

M.P.M.H.Benoit,A.B.Asenjo,H.Sosa

Key ref:

M.P.M.H.Benoit et al. (2018). Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s. Nat Commun, 9, 1662. PubMed id: 29695795

Date:

14-Sep-17 Release date: 02-May-18

Protein chains

Q2XVP4  (TBA1B_PIG) -  Tubulin alpha-1B chain from Sus scrofa

Seq: 451 a.a.

Struc: 439 a.a.

Protein chains

P02554  (TBB_PIG) -  Tubulin beta chain from Sus scrofa

Seq: 445 a.a.

Struc: 425 a.a.*

Protein chain

Q960Z0  (KI10A_DROME) -  Kinesin-like protein Klp10A from Drosophila melanogaster

Seq: 805 a.a.

Struc: 336 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chains A, C: E.C.3.6.5.- - ?????
• Enzyme class 2: Chains B, D, K: 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.

Nat Commun 9:1662 (2018)

PubMed id: 29695795

Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.

M.P.M.H.Benoit, A.B.Asenjo, H.Sosa.

ABSTRACT

Kinesin-13s constitute a distinct group within the kinesin superfamily of motor proteins that promote microtubule depolymerization and lack motile activity. The molecular mechanism by which kinesin-13s depolymerize microtubules and are adapted to perform a seemingly very different activity from other kinesins is still unclear. To address this issue, here we report the near atomic resolution cryo-electron microscopy (cryo-EM) structures of Drosophila melanogaster kinesin-13 KLP10A protein constructs bound to curved or straight tubulin in different nucleotide states. These structures show how nucleotide induced conformational changes near the catalytic site are coupled with movement of the kinesin-13-specific loop-2 to induce tubulin curvature leading to microtubule depolymerization. The data highlight a modular structure that allows similar kinesin core motor-domains to be used for different functions, such as motility or microtubule depolymerization.