The SOUL protein is known to induce apoptosis by provoking the mitochondrial permeability transition, and a sequence homologous with the BH3 (Bcl-2 homology 3) domains has recently been identified in the protein, thus making it a potential new member of the BH3-only protein family. In the present study, we provide NMR, SPR (surface plasmon resonance) and crystallographic evidence that a peptide spanning residues 147–172 in SOUL interacts with the anti-apoptotic protein Bcl-xL. We have crystallized SOUL alone and the complex of its BH3 domain peptide with Bcl-xL, and solved their three-dimensional structures. The SOUL monomer is a single domain organized as a distorted β-barrel with eight anti-parallel strands and two α-helices. The BH3 domain extends across 15 residues at the end of the second helix and eight amino acids in the chain following it. There are important structural differences in the BH3 domain in the intact SOUL molecule and the same sequence bound to Bcl-xL.
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Research Article|
August 12 2011
Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL
Emmanuele Ambrosi;
Emmanuele Ambrosi
1Biocrystallography Laboratory, Department of Biotechnology, University of Verona, Ca Vignal 1, strada Le Grazie 15, 37134 Verona, Italy
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Stefano Capaldi;
Stefano Capaldi
1Biocrystallography Laboratory, Department of Biotechnology, University of Verona, Ca Vignal 1, strada Le Grazie 15, 37134 Verona, Italy
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Michele Bovi;
Michele Bovi
1Biocrystallography Laboratory, Department of Biotechnology, University of Verona, Ca Vignal 1, strada Le Grazie 15, 37134 Verona, Italy
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Gianmaria Saccomani;
Gianmaria Saccomani
1Biocrystallography Laboratory, Department of Biotechnology, University of Verona, Ca Vignal 1, strada Le Grazie 15, 37134 Verona, Italy
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Massimiliano Perduca;
Massimiliano Perduca
1Biocrystallography Laboratory, Department of Biotechnology, University of Verona, Ca Vignal 1, strada Le Grazie 15, 37134 Verona, Italy
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Hugo L. Monaco
Hugo L. Monaco
1
1Biocrystallography Laboratory, Department of Biotechnology, University of Verona, Ca Vignal 1, strada Le Grazie 15, 37134 Verona, Italy
1To whom correspondence should be addressed (email monaco@sci.univr.it).
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Publisher: Portland Press Ltd
Received:
February 10 2011
Revision Received:
May 26 2011
Accepted:
June 06 2011
Accepted Manuscript online:
June 06 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem J (2011) 438 (2): 291–301.
Article history
Received:
February 10 2011
Revision Received:
May 26 2011
Accepted:
June 06 2011
Accepted Manuscript online:
June 06 2011
Citation
Emmanuele Ambrosi, Stefano Capaldi, Michele Bovi, Gianmaria Saccomani, Massimiliano Perduca, Hugo L. Monaco; Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL. Biochem J 1 September 2011; 438 (2): 291–301. doi: https://doi.org/10.1042/BJ20110257
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