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

Panchali Goswami; Cristina Batista Paulino; Dilem Hizlan; Janet Vonck; Özkan Yildiz; Werner Kuehlbrandt

doi:10.1038/emboj.2010.321

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

Panchali Goswami, Cristina Batista Paulino, Dilem Hizlan, Janet Vonck, Özkan Yildiz, Werner Kuehlbrandt

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Abstract

We have determined the structure of the archaeal sodium/proton antiporter NhaP1 at 7 angstrom resolution by electron crystallography of 2D crystals. NhaP1 is a dimer in the membrane, with 13 membrane-spanning a-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 alpha-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 angstrom 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. The EMBO Journal (2011) 30, 439-449. doi:10.1038/emboj.2010.321; Published online 10 December 2010

Original language	English
Pages (from-to)	439-449
Number of pages	10
Journal	The EMBO Journal
Volume	30
DOIs	https://doi.org/10.1038/emboj.2010.321
Publication status	Published - 19-Jan-2011
Externally published	Yes

Keywords

electron microscopy
membrane protein structure
membrane transport
molecular model
monovalent cation/proton antiporters

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Cite this

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

abstract = "We have determined the structure of the archaeal sodium/proton antiporter NhaP1 at 7 angstrom resolution by electron crystallography of 2D crystals. NhaP1 is a dimer in the membrane, with 13 membrane-spanning a-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 alpha-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 angstrom 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. The EMBO Journal (2011) 30, 439-449. doi:10.1038/emboj.2010.321; Published online 10 December 2010",

keywords = "electron microscopy, membrane protein structure, membrane transport, molecular model, monovalent cation/proton antiporters",

author = "Panchali Goswami and {Batista Paulino}, Cristina and Dilem Hizlan and Janet Vonck and {\"O}zkan Yildiz and Werner Kuehlbrandt",

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AU - Goswami, Panchali

AU - Batista Paulino, Cristina

AU - Hizlan, Dilem

AU - Vonck, Janet

AU - Yildiz, Özkan

AU - Kuehlbrandt, Werner

PY - 2011/1/19

Y1 - 2011/1/19

N2 - We have determined the structure of the archaeal sodium/proton antiporter NhaP1 at 7 angstrom resolution by electron crystallography of 2D crystals. NhaP1 is a dimer in the membrane, with 13 membrane-spanning a-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 alpha-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 angstrom 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. The EMBO Journal (2011) 30, 439-449. doi:10.1038/emboj.2010.321; Published online 10 December 2010

AB - We have determined the structure of the archaeal sodium/proton antiporter NhaP1 at 7 angstrom resolution by electron crystallography of 2D crystals. NhaP1 is a dimer in the membrane, with 13 membrane-spanning a-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 alpha-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 angstrom 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. The EMBO Journal (2011) 30, 439-449. doi:10.1038/emboj.2010.321; Published online 10 December 2010

KW - electron microscopy

KW - membrane protein structure

KW - membrane transport

KW - molecular model

KW - monovalent cation/proton antiporters

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DO - 10.1038/emboj.2010.321

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