21CP

Crystal structure of LCDV2 Bcl-2 in complex with the zebrafish BaxA BH3 domain

Summary for 21CP

• Entry DOI: 10.2210/pdb21cp/pdb
• Descriptor: Induced myeloid leukemia cell differentiation protein Mcl-1-like, Apoptosis regulator BAX (3 entities in total)
• Functional Keywords: lymphocystis disease virus, lymphocystis disease virus 2, lcdv, lcdv2, bcl-2, viral bcl-2, baxa, bax, bh3, apoptosis
• Biological source: Lymphocystis disease virus 2; More
• Total number of polymer chains: 2
• Total formula weight: 20293.22

Authors

Ku, B.,Lim, D. (deposition date: 2025-12-08, release date: 2026-10-28)

Primary citation

Lim, D.,Park, S.H.,Choi, J.S.,Shin, H.C.,Kim, S.J.,Ku, B.
Crystal structure of Bcl-2 from lymphocystis disease virus 2 in complex with the BH3 domain of zebrafish BaxA.
J.Microbiol, 64:e2512006-e2512006, 2026

PubMed Abstract: Lymphocystis disease viruses (LCDVs), members of the Lymphocystivirus genus of the Iridoviridae family, infect various freshwater and marine fish species. They cause the chronic disease lymphocystis, which is non-fatal, but substantially reduces the commercial value of the infected fish. To date, four genotypes of LCDV (LCDV1-4) have been identified, all of which encode the viral homologue of B-cell lymphoma 2 (Bcl-2), a key inhibitor of apoptosis. In this study, we performed biochemical and structural analyses of LCDV2 Bcl-2. Binding assays revealed that LCDV2 Bcl-2 exhibits binding selectivity toward BH3 domain-containing zebrafish proteins. It interacted with zBaxA and zNoxa, but not with zBaxB, zBid, or zBeclin 1, distinguishing it from mammalian and herpesviral Bcl-2 proteins. Subsequent structural determination of LCDV2 Bcl-2 in complex with the BH3 domain of zBaxA demonstrated that they interact in a canonical manner, primarily mediated by the BH3 consensus motif residues of zBaxA. In addition, a subpocket formed by two phenylalanine residues in LCDV2 Bcl-2 plays a key role in determining binding selectivity.

PubMed: 42252972
DOI: 10.71150/jm.2512006

Experimental method

X-RAY DIFFRACTION (2.289 Å)