The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized

Chen, Kai-En, Richards, Ayanthi A., Caradoc-Davies, Tom T., Vajjhala, Parimala R., Robin, Gautier, Lua, Linda H. L., Hill, Justine M., Schroder, Kate, Sweet, Matthew J., Kellie, Stuart, Kobe, Bostjan and Martin, Jennifer (2013) The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized. Acta Crystallographica Section D: Biological Crystallography, 69 5: 774-784. doi:10.1107/S0907444913001558

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Author Chen, Kai-En
Richards, Ayanthi A.
Caradoc-Davies, Tom T.
Vajjhala, Parimala R.
Robin, Gautier
Lua, Linda H. L.
Hill, Justine M.
Schroder, Kate
Sweet, Matthew J.
Kellie, Stuart
Kobe, Bostjan
Martin, Jennifer
Title The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized
Journal name Acta Crystallographica Section D: Biological Crystallography   Check publisher's open access policy
ISSN 0907-4449
1399-0047
Publication date 2013
Sub-type Article (original research)
DOI 10.1107/S0907444913001558
Open Access Status File (Publisher version)
Volume 69
Issue 5
Start page 774
End page 784
Total pages 11
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell
Collection year 2014
Language eng
Abstract The caspase recruitment domain (CARD) is present in death-domain superfamily proteins involved in inflammation and apoptosis. BinCARD is named for its ability to interact with Bcl10 and inhibit downstream signalling. Human BinCARD is expressed as two isoforms that encode the same N-terminal CARD region but which differ considerably in their C-termini. Both isoforms are expressed in immune cells, although BinCARD-2 is much more highly expressed. Crystals of the CARD fold common to both had low symmetry (space group P1). Molecular replacement was unsuccessful in this low-symmetry space group and, as the construct contains no methionines, first one and then two residues were engineered to methionine for MAD phasing. The double-methionine variant was produced as a selenomethionine derivative, which was crystallized and the structure was solved using data measured at two wavelengths. The crystal structures of the native and selenomethionine double mutant were refined to high resolution (1.58 and 1.40 Å resolution, respectively), revealing the presence of a cis-peptide bond between Tyr39 and Pro40. Unexpectedly, the native crystal structure revealed that all three cysteines were oxidized. The mitochondrial localization of BinCARD-2 and the susceptibility of its CARD region to redox modification points to the intriguing possibility of a redox-regulatory role.
Keyword Alternative splicing
CARD proteins
Cysteine modification
Methionine mutation for MAD phasing
Mitochondrial localization
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

 
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Created: Tue, 07 May 2013, 08:37:54 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences