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2ZFI

Crystal Structure of the Kif1A Motor Domain Before Mg Release

Summary for 2ZFI
Entry DOI10.2210/pdb2zfi/pdb
Related1I5S 1I6I 1VFV 1VFW 1VFX 1VFZ 2ZFJ 2ZFK 2ZFL 2ZFM
DescriptorKinesin-like protein KIF1A, Kinesin heavy chain isoform 5C, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywordskinesin, alpha and beta protein, enzyme, atpase, p-loop, motor protein, atp-binding, coiled coil, microtubule, nucleotide-binding, transport protein
Biological sourceMus musculus (Mouse)
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Cellular locationCytoplasm, cytoskeleton : P28738
Total number of polymer chains1
Total formula weight41579.72
Authors
Nitta, R.,Okada, Y.,Hirokawa, N. (deposition date: 2008-01-07, release date: 2008-09-23, Last modification date: 2023-11-01)
Primary citationNitta, R.,Okada, Y.,Hirokawa, N.
Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin.
Nat.Struct.Mol.Biol., 15:1067-1075, 2008
Cited by
PubMed 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.
PubMed: 18806800
DOI: 10.1038/nsmb.1487
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

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