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  Atomic structure of the actin:DNase I complex

Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F., & Holmes, K. C. (1990). Atomic structure of the actin:DNase I complex. Nature, 347, 37-44. doi:doi:10.1038/347037a0.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-AD1A-E Version Permalink: https://hdl.handle.net/21.11116/0000-0000-7DB4-9
Genre: Journal Article

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Nature_347_1990_37.pdf (Any fulltext), 796KB
 
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 Creators:
Kabsch, Wolfgang1, 2, Author           
Mannherz, Hans Georg1, Author           
Suck, Dietrich, Author
Pai, Emil F., 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: The atomic models of the complex between rabbit skeletal muscle actin and bovine pancreatic deoxyribonuclease I both in the ATP and ADP forms have been determined by X-ray analysis at an effective resolution of 2.8 A and 3A, respectively. The two structures are very similar. The actin molecule consists of two domains which can be further subdivided into two subdomains. ADP or ATP is located in the cleft between the domains with a calcium ion bound to the beta- or beta- and gamma-phosphates, respectively. The motif of a five-stranded beta sheet consisting of a beta meander and a right handed beta alpha beta unit appears in each domain suggesting that gene duplication might have occurred. These sheets have the same topology as that found in hexokinase.

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Language(s): eng - English
 Dates: 1990-05-181990-07-251990-09-011990-09-06
 Publication Status: Issued
 Pages: 8
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 Rev. Type: Peer
 Identifiers: DOI: doi:10.1038/347037a0
URI: https://www.ncbi.nlm.nih.gov/pubmed/2395459
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Title: Nature
  Abbreviation : Nature
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 347 Sequence Number: - Start / End Page: 37 - 44 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238