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  ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy

Gutsche, I., Mihalache, O., Hegerl, R., Typke, D., & Baumeister, W. (2000). ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy. FEBS Letters, 477(3), 278-282.

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Genre: Journal Article
Alternative Title : FEBS Lett

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Gutsche, I., Author
Mihalache, O.1, Author              
Hegerl, R.1, Author              
Typke, D.1, Author              
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Chaperonin; Thermosome; Cryo-electron microscopy; Atpase cycle; Thermoplasma acidophilum.; Group-ii chaperonin; Thermoplasma-acidophilum; Crystal-structure; Groel; Cct.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
 Abstract: Chaperonins are double-ring protein folding machines fueled by ATP binding and hydrolysis. Conformational rearrangements upon ATPase cycling of the group I chaperonins, typified by the Escherichia coli GroEL/GroES system, have been thoroughly investigated by cryo-electron microscopy and X-ray crystallography. For archaeal group II chaperonins, however, these methods have so far failed to provide a correlation between the structural and the functional states. Here, we show that the conformation of the native alpha beta-thermosome of Thermoplasma acidophilum in vitrified ice is strictly regulated by adenine nucleotides. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved. [References: 18]

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 Dates: 2000
 Publication Status: Published in print
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 Identifiers: eDoc: 318772
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Title: FEBS Letters
  Alternative Title : FEBS Lett
Source Genre: Journal
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Pages: - Volume / Issue: 477 (3) Sequence Number: - Start / End Page: 278 - 282 Identifier: -