3ZFW

Crystal structure of the TPR domain of kinesin light chain 2 in complex with a tryptophan-acidic cargo peptide

Summary for 3ZFW

• Entry DOI: 10.2210/pdb3zfw/pdb
• Descriptor: KINESIN LIGHT CHAIN 2, PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY M MEMBER 2 (2 entities in total)
• Functional Keywords: hydrolase, kinesin-cargo recognition, motor protein, tpr domain, salmonella
• Biological source: MUS MUSCULUS (HOUSE MOUSE); More
• Cellular location: Cytoplasm: Q8IWE5
• Total number of polymer chains: 4
• Total formula weight: 69155.93

Authors

Pernigo, S.,Lamprecht, A.,Steiner, R.A.,Dodding, M.P. (deposition date: 2012-12-12, release date: 2013-04-03, Last modification date: 2024-11-13)

Primary citation

Pernigo, S.,Lamprecht, A.,Steiner, R.A.,Dodding, M.P.
Structural Basis for Kinesin-1:Cargo Recognition.
Science, 340:356-, 2013

PubMed Abstract: Kinesin-mediated cargo transport is required for many cellular functions and plays a key role in pathological processes. Structural information on how kinesins recognize their cargoes is required for a molecular understanding of this fundamental and ubiquitous process. Here, we present the crystal structure of the tetratricopeptide repeat domain of kinesin light chain 2 in complex with a cargo peptide harboring a "tryptophan-acidic" motif derived from SKIP (SifA-kinesin interacting protein), a critical host determinant in Salmonella pathogenesis and a regulator of lysosomal positioning. Structural data together with biophysical, biochemical, and cellular assays allow us to propose a framework for intracellular transport based on the binding by kinesin-1 of W-acidic cargo motifs through a combination of electrostatic interactions and sequence-specific elements, providing direct molecular evidence of the mechanisms for kinesin-1:cargo recognition.

PubMed: 23519214
DOI: 10.1126/SCIENCE.1234264

Experimental method

X-RAY DIFFRACTION (2.9 Å)