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  Structure of the archaeal Na+/H+ antiporter NhaP1 and functional role of transmembrane helix 1

Goswami, P., Paulino, C., Hizlan, D., Vonck, J., Yildiz, Ö., & Kühlbrandt, W. (2011). Structure of the archaeal Na+/H+ antiporter NhaP1 and functional role of transmembrane helix 1. The EMBO Journal, 30(2), 439-449. doi:10.1038/emboj.2010.321.

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 Creators:
Goswami, Panchali1, Author           
Paulino, Cristina1, Author           
Hizlan, Dilem1, Author           
Vonck, Janet1, Author           
Yildiz, Özkan1, Author           
Kühlbrandt, Werner1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Free keywords: electron cryo-microscopy; membrane proteinstructure; membrane transport; molecular model; monova-lent cation/proton antiporters
 Abstract: We have determined the structure of the archaeal sodium/proton antiporter NhaP1 at 7 Å resolution by electron crystallography of 2D crystals. NhaP1 is a dimer in the membrane, with 13 membrane-spanning α-helices per protomer, whereas the distantly related bacterial NhaA has 12. Dimer contacts in the two antiporters are very different, but the structure of a six-helix bundle at the tip of the protomer is conserved. The six-helix bundle of NhaA contains two partially unwound α-helices thought to harbour the ion-translocation site, which is thus similar in NhaP1. A model of NhaP1 based on detailed sequence comparison and the NhaA structure was fitted to the 7 Å map. The additional N-terminal helix 1 of NhaP1, which appears to be an uncleaved signal sequence, is located near the dimer interface. Similar sequences are present in many eukaryotic homologues of NhaP1, including NHE1. Although fully folded and able to dimerize, NhaP1 constructs without helix 1 are inactive. Possible reasons are investigated and discussed.

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Language(s): eng - English
 Dates: 2010-07-282010-11-102010-12-102011-01-19
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/emboj.2010.321
PMID: 21151096
PMC: PMC3025466
 Degree: -

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Title: The EMBO Journal
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 30 (2) Sequence Number: - Start / End Page: 439 - 449 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061_1