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  Structure of a genetically engineered molecular motor

Kliche, W., Fujita-Becker, S., Kollmar, M., Manstein, D. J., & Kull, F. J. (2001). Structure of a genetically engineered molecular motor. EMBO Journal, 20(1), 40-46. doi:10.1093/emboj/20.1.40.

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Genre: Journal Article
Alternative Title : Structure of a genetically engineered molecular motor

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EMBOJ_20_2001_40.pdf (Any fulltext), 306KB
 
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 Creators:
Kliche, Werner1, Author              
Fujita-Becker, Setsuko2, Author              
Kollmar, Martin2, Author              
Manstein, Dietmar J.2, 3, Author              
Kull, F. Jon2, Author              
Affiliations:
1Emeritus Group Bioorganic Chemistry, Max Planck Institute for Medical Research, Max Planck Society, ou_1497711              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
3Dietmar Manstein Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497708              

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Free keywords: α‐actinin; Dictyostelium discoideum; lever arm; myosin; protein engineering
 Abstract: Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the nucleotide-binding region into force-generating movements of larger protein domains. We present the 2.8 A resolution crystal structure of an artificial actin-based motor. By combining the catalytic domain of myosin II with a 130 A conformational amplifier consisting of repeats 1 and 2 of alpha-actinin, we demonstrate that it is possible to genetically engineer single-polypeptide molecular motors with precisely defined lever arm lengths and specific motile properties. Furthermore, our structure shows the consequences of mutating a conserved salt bridge in the nucleotide-binding region. Disruption of this salt bridge, which is known to severely inhibit ATP hydrolysis activity, appears to interfere with formation of myosin's catalytically active 'closed' conformation. Finally, we describe the structure of alpha-actinin repeats 1 and 2 as being composed of two rigid, triple-helical bundles linked by an uninterrupted alpha-helix. This fold is very similar to the previously described structures of alpha-actinin repeats 2 and 3, and alpha-spectrin repeats 16 and 17.

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Language(s): eng - English
 Dates: 2000-09-152000-11-062001-01-152001-01-15
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: EMBO Journal
  Other : EMBO J.
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 20 (1) Sequence Number: - Start / End Page: 40 - 46 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061