PDBsum entry 5fjy

Protein transport

PDB id: 5fjy

Contents

Protein chains

267 a.a.

Ligands

UNK-UNK-UNK-UNK-UNK ×2

UNK-UNK

PDB id:

5fjy

Name:

Protein transport

Title:

Crystal structure of mouse kinesin light chain 2 (residues 161-480)

Structure:

Kinesin light chain 2. Chain: a, b, c. Fragment: tpr domain with n-terminal extension. Synonym: klc2. Engineered: yes. Unknown peptide. Chain: d, e, f. Engineered: yes. Other_details: peptide may be part of tpr n-terminal extension

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

4.00Å R-factor: 0.234 R-free: 0.261

Authors:

S.Pernigo,Y.Y.Yip,A.Sanger,M.Xu,M.P.Dodding,R.A.Steiner

Key ref:

Y.Y.Yip et al. (2016). The light chains of kinesin-1 are autoinhibited. Proc Natl Acad Sci U S A, 113, 2418-2423. PubMed id: 26884162 DOI: 10.1073/pnas.1520817113

Date:

14-Oct-15 Release date: 24-Feb-16

Protein chains

O88448  (KLC2_MOUSE) -  Kinesin light chain 2 from Mus musculus

Seq: 599 a.a.

Struc: 267 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DOI no: 10.1073/pnas.1520817113

Proc Natl Acad Sci U S A 113:2418-2423 (2016)

PubMed id: 26884162

The light chains of kinesin-1 are autoinhibited.

Y.Y.Yip, S.Pernigo, A.Sanger, M.Xu, M.Parsons, R.A.Steiner, M.P.Dodding.

ABSTRACT

The light chains (KLCs) of the microtubule motor kinesin-1 bind cargoes and regulate its activity. Through their tetratricopeptide repeat domain (KLC(TPR)), they can recognize short linear peptide motifs found in many cargo proteins characterized by a central tryptophan flanked by aspartic/glutamic acid residues (W-acidic). Using a fluorescence resonance energy transfer biosensor in combination with X-ray crystallographic, biochemical, and biophysical approaches, we describe how an intramolecular interaction between the KLC2(TPR) domain and a conserved peptide motif within an unstructured region of the molecule, partly occludes the W-acidic binding site on the TPR domain. Cargo binding displaces this interaction, effecting a global conformational change in KLCs resulting in a more extended conformation. Thus, like the motor-bearing kinesin heavy chains, KLCs exist in a dynamic conformational state that is regulated by self-interaction and cargo binding. We propose a model by which, via this molecular switch, W-acidic cargo binding regulates the activity of the holoenzyme.