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  A comparison of the atomic model of f-actin with cryo-electron micrographs of actin and decorated actin

Holmes, K. C., Tirion, M., Popp, D., Lorenz, M., Kabsch, W., & Milligan, R. A. (1993). A comparison of the atomic model of f-actin with cryo-electron micrographs of actin and decorated actin. In Advances in Experimental Biology and Medicine (pp. 15-24). Springer.

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Alternative Title : A comparison of the atomic model of f-actin with cryo-electron micrographs of actin and decorated actin

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AdvExpMedBiol_332_1993_15.pdf (Any fulltext), 1020KB
 
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 Creators:
Holmes, Kenneth C.1, Author           
Tirion, Monique1, Author           
Popp, David, Author
Lorenz, Michael1, 2, Author           
Kabsch, Wolfgang1, 3, Author           
Milligan, Ronald A., Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              
3Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: A comparison of the atomic model of f-actin with cryo-electron micrographs of actin and decorated actin
 Abstract: We compare the atomic model calculated from the crystal structure and the X-ray fiber diagram of orientated F-actin1) with the 3-D reconstructions produced from cryo-electron microscopy of actin2). Out to 30A resolution the two structures are essentially identical. Furthermore, by combining the atomic model with the reconstruction of S1-decorated actin filaments2) one can establish the nature of the actin binding site for myosin in the rigor complex. Each myosin head binds to two actin molecules on two distinct sites. Some of the actin residues involved in each of these binding sites can be identified. Furthermore, the atomic model of actin may be combined with the reconstruction of the S1 decorated thin filament to establish the tropomyosin binding site in the rigor complex. This result is compared with the model of tropomyosin-actin derived from an analysis of the X-ray fibre diagram of a reconstituted thin filament and are shown to be very similar.

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Language(s): eng - English
 Dates: 1993
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666825
Other: 3998
DOI: 10.1007/978-1-4615-2872-2_2
 Degree: -

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Title: Advances in Experimental Biology and Medicine
  Alternative Title : Advances in Experimental Biology and Medicine
Source Genre: Series
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Publ. Info: Springer
Pages: - Volume / Issue: 332 Sequence Number: - Start / End Page: 15 - 24 Identifier: ISBN: 978-1-4613-6245-6
ISBN: 978-1-4615-2872-2