Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing

Sheila C Wang; Argyris Politis; Natalie Di Bartolo; Vassiliy N Bavro; Stephen J Tucker; Paula J Booth; Nelson P Barrera; Carol V Robinson

doi:10.1021/ja104312e

Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing

Sheila C Wang, Argyris Politis, Natalie Di Bartolo, Vassiliy N Bavro, Stephen J Tucker, Paula J Booth, Nelson P Barrera, Carol V Robinson

Chemistry

Research output: Contribution to journal › Article › peer-review

73 Citations (Scopus)

Abstract

Here we examined the gas-phase structures of two tetrameric membrane protein complexes by ion mobility mass spectrometry. The collision cross sections measured for the ion channel are in accord with a compact configuration of subunits, suggesting that the native-like structure can be preserved under the harsh activation conditions required to release it from the detergent micelle into the gas phase. We also found that the quaternary structure of the transporter, which has fewer transmembrane subunits than the ion channel, is less stable once stripped of detergents and bulk water. These results highlight the potential of ion mobility mass spectrometry for characterizing the overall topologies of membrane protein complexes and the structural changes associated with nucleotide, lipid, and drug binding.

Original language	English
Pages (from-to)	15468-15470
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	132
Issue number	44
DOIs	https://doi.org/10.1021/ja104312e
Publication status	Published - 10 Nov 2010

Keywords

Gases
Mass Spectrometry
Membrane Proteins
Models, Molecular
Multiprotein Complexes
Protein Subunits

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10.1021/ja104312e

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title = "Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing",

abstract = "Here we examined the gas-phase structures of two tetrameric membrane protein complexes by ion mobility mass spectrometry. The collision cross sections measured for the ion channel are in accord with a compact configuration of subunits, suggesting that the native-like structure can be preserved under the harsh activation conditions required to release it from the detergent micelle into the gas phase. We also found that the quaternary structure of the transporter, which has fewer transmembrane subunits than the ion channel, is less stable once stripped of detergents and bulk water. These results highlight the potential of ion mobility mass spectrometry for characterizing the overall topologies of membrane protein complexes and the structural changes associated with nucleotide, lipid, and drug binding.",

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author = "Wang, {Sheila C} and Argyris Politis and {Di Bartolo}, Natalie and Bavro, {Vassiliy N} and Tucker, {Stephen J} and Booth, {Paula J} and Barrera, {Nelson P} and Robinson, {Carol V}",

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T1 - Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing

AU - Wang, Sheila C

AU - Politis, Argyris

AU - Di Bartolo, Natalie

AU - Bavro, Vassiliy N

AU - Tucker, Stephen J

AU - Booth, Paula J

AU - Barrera, Nelson P

AU - Robinson, Carol V

PY - 2010/11/10

Y1 - 2010/11/10

N2 - Here we examined the gas-phase structures of two tetrameric membrane protein complexes by ion mobility mass spectrometry. The collision cross sections measured for the ion channel are in accord with a compact configuration of subunits, suggesting that the native-like structure can be preserved under the harsh activation conditions required to release it from the detergent micelle into the gas phase. We also found that the quaternary structure of the transporter, which has fewer transmembrane subunits than the ion channel, is less stable once stripped of detergents and bulk water. These results highlight the potential of ion mobility mass spectrometry for characterizing the overall topologies of membrane protein complexes and the structural changes associated with nucleotide, lipid, and drug binding.

AB - Here we examined the gas-phase structures of two tetrameric membrane protein complexes by ion mobility mass spectrometry. The collision cross sections measured for the ion channel are in accord with a compact configuration of subunits, suggesting that the native-like structure can be preserved under the harsh activation conditions required to release it from the detergent micelle into the gas phase. We also found that the quaternary structure of the transporter, which has fewer transmembrane subunits than the ion channel, is less stable once stripped of detergents and bulk water. These results highlight the potential of ion mobility mass spectrometry for characterizing the overall topologies of membrane protein complexes and the structural changes associated with nucleotide, lipid, and drug binding.

KW - Gases

KW - Mass Spectrometry

KW - Membrane Proteins

KW - Models, Molecular

KW - Multiprotein Complexes

KW - Protein Subunits

U2 - 10.1021/ja104312e

DO - 10.1021/ja104312e

M3 - Article

C2 - 20949939

SN - 0002-7863

VL - 132

SP - 15468

EP - 15470

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 44

ER -

Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing

Abstract

Keywords

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