PDBsum entry 5hnz

Structural protein/motor protein

PDB id: 5hnz

Contents

Protein chains

412 a.a.

426 a.a.

316 a.a.

Ligands

GTP

GDP

TA1

Metals

_MG

PDB id:

5hnz

Name:

Structural protein/motor protein

Title:

Structural basis of backwards motion in kinesin-14: plus-end directed nkn669 in the nucleotide-free state

Structure:

Tubulin alpha-1b chain. Chain: a. Synonym: alpha-tubulin ubiquitous,tubulin k-alpha-1,tubulin alpha- ubiquitous chain. Tubulin beta-2b chain. Chain: b. Protein claret segregational,protein claret segregational, plus-end directed kinesin-1/kinesin-14,protein claret segregational, protein claret segregational.

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Drosophila melanogaster, rattus norvegicus. Fruit fly, rat. Organism_taxid: 7227, 10116. Gene: ncd, ca(nd), cg7831. Expressed in: escherichia coli. Expression_system_taxid: 562.

Authors:

H.Shigematsu,T.Yokoyama,M.Kikkawa,M.Shirouzu,R.Nitta

Key ref:

M.Yamagishi et al. (2016). Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication for Kinesin-14 Motility. Structure, 24, 1322-1334. PubMed id: 27452403 DOI: 10.1016/j.str.2016.05.021

Date:

19-Jan-16 Release date: 10-Aug-16

Protein chain

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

Seq: 451 a.a.

Struc: 412 a.a.*

Protein chain

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

Seq: 445 a.a.

Struc: 426 a.a.*

Protein chain

P20480  (NCD_DROME) -  Protein claret segregational from Drosophila melanogaster

Seq: 700 a.a.

Struc: 316 a.a.*

Protein chain

P56536  (KIF5C_RAT) -  Kinesin heavy chain isoform 5C from Rattus norvegicus

Seq: 955 a.a.

Struc: 316 a.a.*

* PDB and UniProt seqs differ at 205 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chain A: E.C.3.6.5.- - ?????
• Enzyme class 2: Chain B: E.C.?
• Enzyme class 3: Chain K: E.C.3.6.4.- - ?????

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.str.2016.05.021

Structure 24:1322-1334 (2016)

PubMed id: 27452403

Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication for Kinesin-14 Motility.

M.Yamagishi, H.Shigematsu, T.Yokoyama, M.Kikkawa, M.Sugawa, M.Aoki, M.Shirouzu, J.Yajima, R.Nitta.

ABSTRACT

Kinesin-14 is a unique minus-end-directed microtubule-based motor. A swinging motion of a class-specific N-terminal neck helix has been proposed to produce minus-end directionality. However, it is unclear how swinging of the neck helix is driven by ATP hydrolysis utilizing the highly conserved catalytic core among all kinesins. Here, using a motility assay, we show that in addition to the neck helix, the conserved five residues at the C-terminal region in kinesin-14, namely the neck mimic, are necessary to give kinesin-1 an ability to reverse its directionality toward the minus end of microtubules. Our structural analyses further demonstrate that the C-terminal neck mimic, in cooperation with conformational changes in the catalytic core during ATP binding, forms a kinesin-14 bundle with the N-terminal neck helix to swing toward the minus end of microtubules. Thus, the neck mimic plays a crucial role in coupling the chemical ATPase reaction with the mechanical cycle to produce the minus-end-directed motility of kinesin-14.