PDBsum entry 1vfv

Transport protein

PDB id: 1vfv

Contents

Protein chain

324 a.a. *

Ligands

ANP

Metals

_MG

Waters ×247

* Residue conservation analysis

PDB id:

1vfv

Name:

Transport protein

Title:

Crystal structure of the kif1a motor domain complexed with mg-amppnp

Structure:

Protein (fusion protein consisting of kinesin-like protein kif1a, kinesin heavy chain isoform 5c and a his tag. Chain: a. Fragment: motor domain of kinesin-like protein kif1a and residues 329-334 of kinesin heavy chain isoform 5c. Synonym: axonal transporter of synaptic vesicles. Engineered: yes. Other_details: fusion protein comprises residues 1-355 of kinesin- like protein kif1a, and residues 329-334 of kinesin heavy chain

Source:

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

Resolution:

1.85Å R-factor: 0.217 R-free: 0.245

Authors:

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

Key ref:

R.Nitta et al. (2004). KIF1A alternately uses two loops to bind microtubules. Science, 305, 678-683. PubMed id: 15286375 DOI: 10.1126/science.1096621

Date:

19-Apr-04 Release date: 10-Aug-04

Protein chain

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

Seq: 1695 a.a.

Struc: 324 a.a.*

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

DOI no: 10.1126/science.1096621

Science 305:678-683 (2004)

PubMed id: 15286375

KIF1A alternately uses two loops to bind microtubules.

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

ABSTRACT

The motor protein kinesin moves along microtubules, driven by adenosine triphosphate (ATP) hydrolysis. However, it remains unclear how kinesin converts the chemical energy into mechanical movement. We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes). These structures, together with known structures of the ADP-bound state and the adenylyl-(beta,gamma-methylene) diphosphate (AMP-PCP)-bound state, show that kinesin uses two microtubule-binding loops in an alternating manner to change its interaction with microtubules during the ATP hydrolysis cycle; loop L11 is extended in the AMP-PNP structure, whereas loop L12 is extended in the ADP structure. ADP-vanadate displays an intermediate structure in which a conformational change in two switch regions causes both loops to be raised from the microtubule, thus actively detaching kinesin.

Selected figure(s)

Figure 2.
Fig. 2. Crystal structures of KIF1A. (A) The AMP-PNP form of KIF1A. The switch I, switch II, and neck-linker regions are highlighted in red. (B) Superposition of AMP-PNP, ADP-AlFx, ADP-Vi, and ADP structures. The AMP-PNP, ADP-AlFx, ADP-Vi, and ADP forms are shown in red, blue, green, and yellow, respectively.

Figure 3.
Fig. 3. The conformational changes that occur in the two switch regions and the neck-linker region during ATP hydrolysis. (A to D) AMP-PCP (A), AMP-PNP (B), ADP-AlFx (C), and ADP-Vi (D) forms are shown in light brown, red, blue, and green, respectively. These panels are seen from the upper right in Fig. 2A (indicated by the black arrow). Nucleotides and the coordinating residues around them are shown as ball-and-stick models. Missing C-terminal residues and loops are shown by dashed lines. The structural details around the nucleotide-binding pocket are also shown in figs. S2 to S4 (46). (E and F) The conserved salt bridge between Glu170 and Arg316 (enclosed by a red circle), shown in ball-and-stick models in the AMP-PNP (E) and ADP-Vi (F) forms. Loop L8 and the switch II cluster are shown in dark blue and dark red, respectively. Nucleotides are shown as space-filling models.

The above figures are reprinted by permission from the AAAs: Science (2004, 305, 678-683) copyright 2004.

Figures were selected by the author.