PDBsum entry 3j2u

Motor protein

PDB id: 3j2u

Contents

Protein chains

309 a.a.

412 a.a.

426 a.a.

PDB id:

3j2u

Name:

Motor protein

Title:

Kinesin-13 klp10a hd in complex with cs-tubulin and a microtubule

Structure:

Kinesin-like protein klp10a. Chain: k. Fragment: head domain (unp residues 279-615). Synonym: kinesin-like protein at cytological position 10a. Engineered: yes. Tubulin alpha-1a chain. Chain: a, c. Synonym: alpha-tubulin 1, tubulin alpha-1 chain. Tubulin beta-2b chain.

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: klp10a, cg1453. Expressed in: escherichia coli. Expression_system_taxid: 562. Bos taurus. Bovine. Organism_taxid: 9913.

Authors:

A.B.Asenjo,C.Chatterjee,D.Tan,V.Depaoli,W.J.Rice,R.Diaz-Avalos, M.Silvestry,H.Sosa

Key ref:

A.B.Asenjo et al. (2013). Structural model for tubulin recognition and deformation by kinesin-13 microtubule depolymerases. Cell Rep, 3, 759-768. PubMed id: 23434508 DOI: 10.1016/j.celrep.2013.01.030

Date:

10-Jan-13 Release date: 06-Mar-13

Protein chain

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

Seq: 805 a.a.

Struc: 309 a.a.

Protein chains

P81947  (TBA1B_BOVIN) -  Tubulin alpha-1B chain from Bos taurus

Seq: 451 a.a.

Struc: 412 a.a.*

Protein chains

Q6B856  (TBB2B_BOVIN) -  Tubulin beta-2B chain from Bos taurus

Seq: 445 a.a.

Struc: 426 a.a.*

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

Enzyme reactions

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

DOI no: 10.1016/j.celrep.2013.01.030

Cell Rep 3:759-768 (2013)

PubMed id: 23434508

Structural model for tubulin recognition and deformation by kinesin-13 microtubule depolymerases.

A.B.Asenjo, C.Chatterjee, D.Tan, V.DePaoli, W.J.Rice, R.Diaz-Avalos, M.Silvestry, H.Sosa.

ABSTRACT

To elucidate the structural basis of the mechanism of microtubule depolymerization by kinesin-13s, we analyzed complexes of tubulin and the Drosophila melanogaster kinesin-13 KLP10A by electron microscopy (EM) and fluorescence polarization microscopy. We report a nanometer-resolution (1.1 nm) cryo-EM three-dimensional structure of the KLP10A head domain (KLP10AHD) bound to curved tubulin. We found that binding of KLP10AHD induces a distinct tubulin configuration with displacement (shear) between tubulin subunits in addition to curvature. In this configuration, the kinesin-binding site differs from that in straight tubulin, providing an explanation for the distinct interaction modes of kinesin-13s with the microtubule lattice or its ends. The KLP10AHD-tubulin interface comprises three areas of interaction, suggesting a crossbow-type tubulin-bending mechanism. These areas include the kinesin-13 family conserved KVD residues, and as predicted from the crossbow model, mutating these residues changes the orientation and mobility of KLP10AHDs interacting with the microtubule.