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  The actin fold

Kabsch, W., & Holmes, K. C. (1995). The actin fold. The FASEB Journal, 9(2), 167-174. Retrieved from 7781919.

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Genre: Journal Article
Alternative Title : The actin fold

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FASEBJ_9_1995_167.pdf (Any fulltext), 2MB
 
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 Creators:
Kabsch, Wolfgang1, 2, Author              
Holmes, Kenneth C.1, 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              

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Free keywords: heat-shock proteins ; hexokinase ; glycerol kinase ; ATP
 Abstract: X-ray structure analysis of actin and of the NH2-terminal domain of the heat-shock cognate protein Hsc70 has revealed an unexpected extensive structural similarity between these two molecules. Despite the absence of significant similarity of their amino acid sequences, both proteins share the same core architecture and a common nucleotide binding site resembling the structure of hexokinase. All three are ATPases or kinases and bind ATP in association with Mg2+ or Ca2+. The common fold consists of two alpha/beta domains, which are connected by a putative hinge with an ATP-binding site situated between the domains. Each domain contains a five-stranded beta-sheet of identical topology, which suggests that the molecules may have evolved by gene duplication. From a comparison of the three aligned structures, a fingerprint sequence of the adenine nucleotide binding pocket was derived, which predicted that members of the glycerol kinase family should also have a similar fold of their nucleotide binding domain. This was later confirmed when the X-ray structure was published. Data base search with a refined consensus sequence has retrieved other sugar kinases, as well as the prokaryotic cell cycle proteins FtsA, MreB, and StbA, and two Escherichia coli phosphatases. These proteins are predicted to possess a structure similar to actin in the common core region. As exemplified for actin, Hsc70, and glycerol kinase, the diversity of biological function is provided by the polymorphism of the loops joining the beta-strands and helices in the core region and by inserted domains that show high variability.

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Language(s): eng - English
 Dates: 1995-02-01
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666731
URI: 7781919
URI: http://www.ncbi.nlm.nih.gov/pubmed/7781919
URI: http://www.fasebj.org/cgi/content/abstract/9/2/167
Other: 4159
 Degree: -

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Title: The FASEB Journal
  Other : FASEB J.
Source Genre: Journal
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Publ. Info: Bethesda, Md. : The Federation
Pages: - Volume / Issue: 9 (2) Sequence Number: - Start / End Page: 167 - 174 Identifier: ISSN: 0892-6638
CoNE: https://pure.mpg.de/cone/journals/resource/954927535970_1