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  Comparison of H+-ATPase and Ca2+-ATPase suggests that a large conformational change initiates P-type ion pump reaction cycles

Stokes, D. L., Auer, M., Zhang Peijun, P., & Kühlbrandt, W. (1999). Comparison of H+-ATPase and Ca2+-ATPase suggests that a large conformational change initiates P-type ion pump reaction cycles. Current Biology, 9(13), 672-679. doi:10.1016/S0960-9822(99)80307-8.

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 Creators:
Stokes, David L.1, Author
Auer, Manfred2, Author           
Zhang Peijun, Peijun3, Author
Kühlbrandt, Werner2, Author                 
Affiliations:
1Department of Cell Biology, Skirball Institute for Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, New York, 10016, USA, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
3Department of Cell Biology, Skirball Institute for Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, New York 10016, National Institutes of Health, NIDDK, LCBB, Building 8, 8 Center Drive, Bethesda, Maryland 20892, USA, ou_persistent22              

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 Abstract: Background: Structures have recently been solved at 8 å resolution for both Ca2+-ATPase from rabbit sarcoplasmic reticulum and H+-ATPase from Neurospora crassa. These cation pumps are two distantly related members of the family of P-type ATPases, which are thought to use similar mechanisms to generate ATP-dependent ion gradients across a variety of cellular membranes. We have undertaken a detailed comparison of the two structures in order to describe their similarities and differences as they bear on their mechanism of active transport.

Results: Our first important finding was that the arrangement of 10 transmembrane helices was remarkably similar in the two molecules. This structural homology strongly supports the notion that these pumps use the same basic mechanism to transport their respective ions. Despite this similarity in the membrane-spanning region, the cytoplasmic regions of the two molecules were very different, both in their disposition relative to the membrane and in the juxtaposition of their various subdomains.

Conclusions: On the basis of the crystallization conditions, we propose that these two crystal structures represent different intermediates in the transport cycle, distinguished by whether cations are bound to their transport sites. Furthermore, we propose that the corresponding conformational change (E2 to E1 ) has two components: the first is an inclination of the main cytoplasmic mass by 20° relative to the membrane-spanning domain; the second is a rearrangement of the domains comprising the cytoplasmic part of the molecules. Accordingly, we present a rough model for this important conformational change, which relays the effects of cation binding within the membrane-spanning domain to the nucleotide-binding site, thus initiating the transport cycle.

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Language(s): eng - English
 Dates: 1999-05-241999-04-061999-05-242000-01-271999-07
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0960-9822(99)80307-8
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Title: Current Biology
  Other : Curr. Biol.
Source Genre: Journal
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Publ. Info: London, UK : Cell Press
Pages: - Volume / Issue: 9 (13) Sequence Number: - Start / End Page: 672 - 679 Identifier: ISSN: 0960-9822
CoNE: https://pure.mpg.de/cone/journals/resource/954925579107