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  Role of the salt-bridge between switch-1 and switch-2 of Dictyostelium myosin

Furch, M., Fujita-Becker, S., Geeves, M. A., Holmes, K. C., & Manstein, D. J. (1999). Role of the salt-bridge between switch-1 and switch-2 of Dictyostelium myosin. Journal of Molecular Biology (London), 290(3), 797-809. doi:10.1006/jmbi.1999.2921.

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Genre: Journal Article
Alternative Title : Role of the salt-bridge between switch-1 and switch-2 of Dictyostelium myosin

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JMolBiol_290_1999_797.pdf (Any fulltext), 356KB
 
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Furch, Marcus1, Author              
Fujita-Becker, Setsuko1, Author              
Geeves, Michael A., Author
Holmes, Kenneth C.1, Author              
Manstein, Dietmar J.1, Author              
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: kinetics; recombinant protein; molecular motor; ATP hydrolysis; actomyosin
 Abstract: Motifs N2 and N3, also referred to as switch-1 and switch-2, form part of the active site of molecular motors such as myosins and kinesins. In the case of myosin, N3 is thought to act as a γ-phosphate sensor and moves almost 6 Å relative to N2 during the catalysed turnover of ATP, opening and closing the active site surrounding the γ-phosphate. The closed form seems to be necessary for hydrolysis and is stabilised by the formation of a salt-bridge between an arginine residue in N2 and a glutamate residue in N3. We examined the role of this salt-bridge in Dictyostelium discoideum myosin. Myosin motor domains with mutations E459R or R238E, that block salt-bridge formation, show defects in nucleotide-binding, reduced rates of ATP hydrolysis and a tenfold reduction in actin affinity. Inversion of the salt-bridge in double-mutant M765-IS eliminates most of the defects observed for the single mutants. With the exception of a 2,500-fold higherKM value for ATP, the double-mutant displayed enzymatic and functional properties very similar to those of the wild-type protein. Our results reveal that, independent of its orientation, the salt-bridge is required to support efficient ATP hydrolysis, normal communication between different functional regions of the myosin head, and motor function

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 290 (3) Sequence Number: - Start / End Page: 797 - 809 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042