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  Structure of the regulatory domain of scallop myosin at 2.8 Ä resolution

Xie, X., Harrison, D. H., Schlichting, I., Sweet, R. M., Kalabokis, V. N., Szent−Gyorgyi, A. G., et al. (1994). Structure of the regulatory domain of scallop myosin at 2.8 Ä resolution. Nature, 368(6469), 306-312. doi:10.1038/368306a0.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-A930-5 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002D-B1E6-F
Genre: Journal Article

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Nature_368_2004_306.pdf (Any fulltext), 956KB
 
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https://www.nature.com/nature/journal/v368/n6469/pdf/368306a0.pdf (Any fulltext)
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https://doi.org/10.1038/368306a0 (Any fulltext)
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 Creators:
Xie, X., Author
Harrison, D. H., Author
Schlichting, Ilme1, 2, Author           
Sweet, Robert M., Author
Kalabokis, V. N., Author
Szent−Gyorgyi, A. G., Author
Cohen, C., Author
Affiliations:
1Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society, ou_1856341              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 Å resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca2+-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.

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Language(s): eng - English
 Dates: 1993-08-311994-01-111994-03-24
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665690
DOI: 10.1038/368306a0
URI: http://www.nature.com/cgi-taf/DynaPage.taf?file%3D%2Fnature%2Fjournal%2Fv368%2Fn6469%2Ffull%2F368306a0.html%26filetype%3Dpdf
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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 368 (6469) Sequence Number: - Start / End Page: 306 - 312 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238