3R8J

Crystal structure of human SOUL protein (orthorhombic form)

Summary for 3R8J

• Entry DOI: 10.2210/pdb3r8j/pdb
• Related: 3R85 3R8K
• Descriptor: Heme-binding protein 2, PHOSPHATE ION (3 entities in total)
• Functional Keywords: hebp family, soul protein, apoptosis
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q9Y5Z4
• Total number of polymer chains: 2
• Total formula weight: 47421.47

Authors

Ambrosi, E.K.,Capaldi, S.,Bovi, M.,Saccomani, G.,Perduca, M.,Monaco, H.L. (deposition date: 2011-03-24, release date: 2011-06-29, Last modification date: 2024-02-21)

Primary citation

Ambrosi, E.,Capaldi, S.,Bovi, M.,Saccomani, G.,Perduca, M.,Monaco, H.L.
Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL.
Biochem.J., 438:291-301, 2011

PubMed Abstract: 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.

PubMed: 21639858
DOI: 10.1042/BJ20110257

Experimental method

X-RAY DIFFRACTION (1.6 Å)