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  Rotary and unidirectional metal shadowing of VAT: Localization of the substrate-binding domain

Rockel, B., Guckenberger, R., Gross, H., Tittmann, P., & Baumeister, W. (2000). Rotary and unidirectional metal shadowing of VAT: Localization of the substrate-binding domain. Journal of Structural Biology, 132(2), 162-168.

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Genre: Journal Article
Alternative Title : J. Struct. Biol

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 Creators:
Rockel, B.1, Author              
Guckenberger, R.1, Author              
Gross, H., Author
Tittmann, P., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Relief reconstruction; Rotary shadowing; Unidirectional shadowing; Vcp-like atpase of thermoplasma.; Sensitive fusion protein; Archaeon thermoplasma-acidophilum; Cdc48/p97 atpase homolog; Crystal-structure; Terminal domain; Electron-microscopy; Aaa atpase; Nsf; Particles; Family.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
 Abstract: AAA-ATPases have important roles in manifold cellular processes. VAT (valosine-containing protein-like ATPase of Thermoplasma acidophilum), a hexameric archaeal member of this family, has the tripartite domain structure N-D1-D2 that is characteristic of many members of this family. N, the N-terminal domain of 20.5 kDa, has been implicated in substrate binding. We have applied rotary and unidirectional shadowing to VAT and an N-terminally deleted mutant, VAT(DeltaN), in order to map the location of this domain. For the analysis of data derived from unidirectionally shadowed samples we used a new approach combining eigenvector analysis with surface relief reconstruction. Averages of rotary shadowed particles as well as relief reconstructions map the N-terminal domains to the periphery of the hexameric complex and reveal their bipartite structure. Thus, this method appears to be well suited to study the conformational changes that occur during the functional cycle of the protein. (C) 2000 Academic Press. [References: 31]

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 Dates: 2000
 Publication Status: Published in print
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 Identifiers: eDoc: 318518
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Title: Journal of Structural Biology
  Alternative Title : J. Struct. Biol
Source Genre: Journal
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Pages: - Volume / Issue: 132 (2) Sequence Number: - Start / End Page: 162 - 168 Identifier: -