High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population

Johann Schredelseker; Aviv Paz; Carlos J. López; Christian Altenbach; Calvin S. Leung; Maria K. Drexler; Jau Nian Chen; Wayne L. Hubbell; Jeff Abramson

doi:10.1074/jbc.M113.497438

High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population

Johann Schredelseker
, Aviv Paz
, Carlos J. López
, Christian Altenbach
, Calvin S. Leung
, Maria K. Drexler
, Jau Nian Chen
, Wayne L. Hubbell
, Jeff Abramson

Department of Structural Biology

Ludwig Maximilian University of Munich
University of California at Los Angeles
Tata Institute of Fundamental Research

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

131 Scopus citations

Abstract

Background: Biochemical characterization of voltage-dependent anion channel 2 (VDAC2) is limited due to an inability to obtain functional protein. Results: The crystal structure ofVDAC2suggests a dimer interface that is confirmed by double electron-electron resonance and cross-linking. Conclusion: zfVDAC2 has a fractional dimeric population. Significance: VDAC isoforms are structurally similar, but this study has identified a number of hot spots that require further exploration.

Original language	English
Pages (from-to)	12566-12577
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	289
Issue number	18
DOIs	https://doi.org/10.1074/jbc.M113.497438
State	Published - 2014

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10.1074/jbc.M113.497438

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Schredelseker, J., Paz, A., López, C. J., Altenbach, C., Leung, C. S., Drexler, M. K., Chen, J. N., Hubbell, W. L., & Abramson, J. (2014). High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population. Journal of Biological Chemistry, 289(18), 12566-12577. https://doi.org/10.1074/jbc.M113.497438

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title = "High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population",

abstract = "Background: Biochemical characterization of voltage-dependent anion channel 2 (VDAC2) is limited due to an inability to obtain functional protein. Results: The crystal structure ofVDAC2suggests a dimer interface that is confirmed by double electron-electron resonance and cross-linking. Conclusion: zfVDAC2 has a fractional dimeric population. Significance: VDAC isoforms are structurally similar, but this study has identified a number of hot spots that require further exploration.",

author = "Johann Schredelseker and Aviv Paz and L{\'o}pez, \{Carlos J.\} and Christian Altenbach and Leung, \{Calvin S.\} and Drexler, \{Maria K.\} and Chen, \{Jau Nian\} and Hubbell, \{Wayne L.\} and Jeff Abramson",

year = "2014",

doi = "10.1074/jbc.M113.497438",

language = "English",

volume = "289",

pages = "12566--12577",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

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Schredelseker, J, Paz, A, López, CJ, Altenbach, C, Leung, CS, Drexler, MK, Chen, JN, Hubbell, WL & Abramson, J 2014, 'High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population', Journal of Biological Chemistry, vol. 289, no. 18, pp. 12566-12577. https://doi.org/10.1074/jbc.M113.497438

TY - JOUR

T1 - High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population

AU - Schredelseker, Johann

AU - Paz, Aviv

AU - López, Carlos J.

AU - Altenbach, Christian

AU - Leung, Calvin S.

AU - Drexler, Maria K.

AU - Chen, Jau Nian

AU - Hubbell, Wayne L.

AU - Abramson, Jeff

PY - 2014

Y1 - 2014

N2 - Background: Biochemical characterization of voltage-dependent anion channel 2 (VDAC2) is limited due to an inability to obtain functional protein. Results: The crystal structure ofVDAC2suggests a dimer interface that is confirmed by double electron-electron resonance and cross-linking. Conclusion: zfVDAC2 has a fractional dimeric population. Significance: VDAC isoforms are structurally similar, but this study has identified a number of hot spots that require further exploration.

AB - Background: Biochemical characterization of voltage-dependent anion channel 2 (VDAC2) is limited due to an inability to obtain functional protein. Results: The crystal structure ofVDAC2suggests a dimer interface that is confirmed by double electron-electron resonance and cross-linking. Conclusion: zfVDAC2 has a fractional dimeric population. Significance: VDAC isoforms are structurally similar, but this study has identified a number of hot spots that require further exploration.

UR - https://www.scopus.com/pages/publications/84899732005

U2 - 10.1074/jbc.M113.497438

DO - 10.1074/jbc.M113.497438

M3 - Article

C2 - 24627492

AN - SCOPUS:84899732005

SN - 0021-9258

VL - 289

SP - 12566

EP - 12577

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 18

ER -

High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population

Abstract

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