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  Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein

Flaherty, K. M., McKay, D. B., Kabsch, W., & Holmes, K. C. (1991). Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proceedings of the National Academy of Sciences of the United States of America, 88(11), 5041-5045. Retrieved from http://www.pnas.org/content/88/11/5041.

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 Creators:
Flaherty, K. M., Author
McKay, D. B., Author
Kabsch, Wolfgang1, 2, Author              
Holmes, Kenneth C.1, 3, 4, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
3Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society, ou_1497735              
4Muscle Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497731              

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 Abstract: Although there is very little sequence identity between the two proteins, the structures of rabbit skeletal muscle actin (375-amino acid residues) and the 44-kDa ATPase fragment of the bovine 70-kDa heat shock cognate protein (HSC70; 386 residues) are very similar. The alpha-carbon positions of 241 pairs of amino acid residues that are structurally equivalent within the two proteins can be superimposed with a root-mean-square difference in distance of 2.3 A; of these, 39 residues are identical, and 56 are conservative substitutions. In addition, the conformations of ADP are very similar in both proteins. A local sequence "fingerprint," which may be diagnostic of the adenine nucleotide beta-phosphate-binding pocket, has been derived. The fingerprint identifies members of the glycerol kinase family as candidates likely to have a similar structure in their nucleotide-binding domains. The structural differences between the two molecules mainly occur in loop regions of actin known to be involved in interactions with other monomers in the actin filament or in the binding of myosin; the corresponding regions in heat shock proteins may have functions that are as yet undetermined. Placing the Ca2+ ATP of actin on the ATPase fragment structure suggests Asp-206 (corresponding to His-161 of actin) as a candidate proton acceptor for the ATPase reaction.

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Language(s): eng - English
 Dates: 1991-01-141991-03-081991-06-01
 Publication Status: Published in print
 Pages: 5
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 Rev. Type: Peer
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proceedings of the National Academy of Sciences of the USA
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 88 (11) Sequence Number: - Start / End Page: 5041 - 5045 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230