The Cryo-EM Structure of the CorA channel from Methanocaldococcus jannaschii in low magnesium conditions.Citation formats

  • External authors:
  • Robert M. Cleverley
  • James Kean
  • Chitra A. Shintre

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The Cryo-EM Structure of the CorA channel from Methanocaldococcus jannaschii in low magnesium conditions. / Cleverley, Robert M.; Kean, James; Shintre, Chitra A.; Baldock, Clair; Derrick, Jeremy P.; Ford, Robert C.; Prince, Stephen M.

In: Biochimica et Biophysica Acta. Biomembranes, Vol. 1848, No. 10 Pt A, 01.10.2015, p. 2206-2215.

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Cleverley RM, Kean J, Shintre CA, Baldock C, Derrick JP, Ford RC et al. The Cryo-EM Structure of the CorA channel from Methanocaldococcus jannaschii in low magnesium conditions. Biochimica et Biophysica Acta. Biomembranes. 2015 Oct 1;1848(10 Pt A):2206-2215. https://doi.org/10.1016/j.bbamem.2015.06.002

Author

Cleverley, Robert M. ; Kean, James ; Shintre, Chitra A. ; Baldock, Clair ; Derrick, Jeremy P. ; Ford, Robert C. ; Prince, Stephen M. / The Cryo-EM Structure of the CorA channel from Methanocaldococcus jannaschii in low magnesium conditions. In: Biochimica et Biophysica Acta. Biomembranes. 2015 ; Vol. 1848, No. 10 Pt A. pp. 2206-2215.

Bibtex

@article{acdc1fcd4c6d42f3b4c56a79a5a22814,
title = "The Cryo-EM Structure of the CorA channel from Methanocaldococcus jannaschii in low magnesium conditions.",
abstract = "CorA channels are responsible for the uptake of essential magnesium ions by bacteria. X-ray crystal structures have been resolved for two full-length CorA channels, each in a non-conducting state with magnesium ions bound to the protein: These structures reveal a homo-pentameric quaternary structure with approximate 5-fold rotational symmetry about a central pore axis. We report the structure of the detergent solubilized Methanocaldococcus jannaschii CorA channel determined by Cryo-electron microscopy and Single Particle Averaging, supported by Small Angle X-ray scattering and X-ray crystallography. This structure also shows a pentameric channel but with a highly asymmetric domain structure. The asymmetry of the domains includes differential separations between the trans-membrane segments, which reflects mechanical coupling of the cytoplasmic domain to the trans-membrane domain. This structure therefore reveals an important aspect of the gating mechanism of CorA channels by providing an indication of how the absence of magnesium ions leads to major structural changes.",
keywords = "Ion channel, Channel gating, Cryo-electron microscopy, Membrane protein",
author = "Cleverley, {Robert M.} and James Kean and Shintre, {Chitra A.} and Clair Baldock and Derrick, {Jeremy P.} and Ford, {Robert C.} and Prince, {Stephen M.}",
year = "2015",
month = oct,
day = "1",
doi = "10.1016/j.bbamem.2015.06.002",
language = "English",
volume = "1848",
pages = "2206--2215",
journal = "Biochimica et Biophysica Acta - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier BV",
number = "10 Pt A",

}

RIS

TY - JOUR

T1 - The Cryo-EM Structure of the CorA channel from Methanocaldococcus jannaschii in low magnesium conditions.

AU - Cleverley, Robert M.

AU - Kean, James

AU - Shintre, Chitra A.

AU - Baldock, Clair

AU - Derrick, Jeremy P.

AU - Ford, Robert C.

AU - Prince, Stephen M.

PY - 2015/10/1

Y1 - 2015/10/1

N2 - CorA channels are responsible for the uptake of essential magnesium ions by bacteria. X-ray crystal structures have been resolved for two full-length CorA channels, each in a non-conducting state with magnesium ions bound to the protein: These structures reveal a homo-pentameric quaternary structure with approximate 5-fold rotational symmetry about a central pore axis. We report the structure of the detergent solubilized Methanocaldococcus jannaschii CorA channel determined by Cryo-electron microscopy and Single Particle Averaging, supported by Small Angle X-ray scattering and X-ray crystallography. This structure also shows a pentameric channel but with a highly asymmetric domain structure. The asymmetry of the domains includes differential separations between the trans-membrane segments, which reflects mechanical coupling of the cytoplasmic domain to the trans-membrane domain. This structure therefore reveals an important aspect of the gating mechanism of CorA channels by providing an indication of how the absence of magnesium ions leads to major structural changes.

AB - CorA channels are responsible for the uptake of essential magnesium ions by bacteria. X-ray crystal structures have been resolved for two full-length CorA channels, each in a non-conducting state with magnesium ions bound to the protein: These structures reveal a homo-pentameric quaternary structure with approximate 5-fold rotational symmetry about a central pore axis. We report the structure of the detergent solubilized Methanocaldococcus jannaschii CorA channel determined by Cryo-electron microscopy and Single Particle Averaging, supported by Small Angle X-ray scattering and X-ray crystallography. This structure also shows a pentameric channel but with a highly asymmetric domain structure. The asymmetry of the domains includes differential separations between the trans-membrane segments, which reflects mechanical coupling of the cytoplasmic domain to the trans-membrane domain. This structure therefore reveals an important aspect of the gating mechanism of CorA channels by providing an indication of how the absence of magnesium ions leads to major structural changes.

KW - Ion channel

KW - Channel gating

KW - Cryo-electron microscopy

KW - Membrane protein

U2 - 10.1016/j.bbamem.2015.06.002

DO - 10.1016/j.bbamem.2015.06.002

M3 - Article

C2 - 26051127

VL - 1848

SP - 2206

EP - 2215

JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

SN - 0005-2736

IS - 10 Pt A

ER -