PDBsum entry 2zfk

Transport protein

PDB id: 2zfk

Contents

Protein chain

321 a.a. *

Ligands

ADP

TRS ×2

Metals

_MG

Waters ×27

* Residue conservation analysis

PDB id:

2zfk

Name:

Transport protein

Title:

Crystal structure of the kif1a motor domain during mg release: mg- releasing transition-2

Structure:

Kinesin-like protein kif1a, kinesin heavy chain isoform 5c. Chain: a. Fragment: kif1a (residues 1-355), kif5c (residues 329-334). Synonym: axonal transporter of synaptic vesi cles, kinesin heavy chain neuron-specific 2. Engineered: yes. Other_details: fusion protein comprises residues 1-355 of kinesin- like protein kif1a, and residues 329-334 of kinesin heavy chain isoform 5c, and c-terminal tail with sequence hhhhh

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.61Å R-factor: 0.292 R-free: 0.349

Authors:

R.Nitta,Y.Okada,N.Hirokawa

Key ref:

R.Nitta et al. (2008). Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin. Nat Struct Biol, 15, 1067-1075. PubMed id: 18806800 DOI: 10.1038/nsmb.1487

Date:

08-Jan-08 Release date: 23-Sep-08

Protein chain

P33173  (KIF1A_MOUSE) -  Kinesin-like protein KIF1A from Mus musculus

Seq: 1695 a.a.

Struc: 321 a.a.

DOI no: 10.1038/nsmb.1487

Nat Struct Biol 15:1067-1075 (2008)

PubMed id: 18806800

Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin.

R.Nitta, Y.Okada, N.Hirokawa.

ABSTRACT

Mg-ADP release is considered to be a crucial process for the regulation and motility of kinesin. To gain insight into the structural basis of this process, we solved the atomic structures of kinesin superfamily protein-1A (KIF1A) during and after Mg(2+) release. On the basis of new structural and mutagenesis data, we propose a model mechanism for microtubule activation of Mg-ADP release from KIF1A. In our model, a specific interaction between loop L7 of KIF1A and beta-tubulin reconfigures the KIF1A active site by shifting the relative positions of switches I and II. This leads to the sequential release of a group of water molecules that sits over the Mg(2+) in the active site, followed by Mg(2+) and finally the ADP. We further propose that this set of events is linked to a strain-dependent docking of the neck linker to the motor core, which produces a two-step power stroke.

Selected figure(s)

Figure 2.
(a) Superposition (with the use of the C atoms of P-loop) of the five structures, K-Mg-ADP (red), transition 1 (orange), transition 2 (yellow green), transition 3 (cyan) and K-ADP (blue) are shown, seen from the microtubule binding side. (b) The r.m.s. deviations between the K-Mg-ADP and the K-ADP states are indicated by the colorings: higher r.m.s. deviations are shown in warmer colors and lower values in cooler colors.

Figure 8.
See text for details.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2008, 15, 1067-1075) copyright 2008.

Figures were selected by the author.