The Structure of the Nucleotide-Binding Site of Kinesin
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J. Müller
, A. Marx , S. Sack , Y.-H. Song and E. Mandelkow
Abstract
Kinesin is a microtubule-based motor protein responsible for anterograde transport of vesicles and organelles in nerve axons and other cell types. The energy necessary for this transport is derived from the hydrolysis of ATP which is thought to induce conformational changes in the protein. We have solved the X-ray crystal structures of rat brain kinesin in three conditions intended to mimic different nucleotide states: (1) with ADP bound to the nucleotide-binding site, (2) with bound ADP in the presence of AlF4−, and (3) with ADP hydrolyzed to AMP by apyrase. In contrast to analogous cases observed in GTP-binding proteins or the muscle motor myosin, the structure of kinesin remained nearly unchanged. This highlights the stability of kinesin's ADP state in the absence of microtubules. Surprisingly, even after hydrolysis of ADP to AMP by apyrase a strong density peak remains at the position of the β-phosphate which is compatible either with a phosphate or a sulfate from the solvent and appears to stabilize the nucleotide-binding pocket through several hydrogen bonds.
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
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- Mutations of Calcium Channel beta Subunit Genes in Mice
- Agonist-Stimulated Pathways of Calcium Signaling in Pancreatic Acinar Cells
- Some of the Early Events Underlying Th2. Cell Maturation and Susceptibility to Leishmania major Infection in BALB/c Mice
- Universal and Unique Features of Kinesin Motors: Insights from a Comparison of Fungal and Animal Conventional Kinesins
- Elementary Steps in Protein Folding
- Molecular Reaction Mechanisms of Proteins Monitored by Time-Resolved FTIR-Spectroscopy
- Sugars as Signal Molecules in Plant Seed Development
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