8U0R
The crystal structure of protein A21, a component of the conserved poxvirus entry-fusion complex
Summary for 8U0R
| Entry DOI | 10.2210/pdb8u0r/pdb |
| Descriptor | Virion membrane protein A21, 2-(2-METHOXYETHOXY)ETHANOL, 2-AMINO-ETHANETHIOL, ... (17 entities in total) |
| Functional Keywords | poxvirus, entry-fusion complex, poxvirus a21 protein, vaccinia virus, viral protein |
| Biological source | Vaccinia virus Western Reserve |
| Total number of polymer chains | 6 |
| Total formula weight | 70886.21 |
| Authors | Diesterbeck, U.,Gittis, A.G.,Garboczi, D.N.,Moss, B. (deposition date: 2023-08-29, release date: 2024-09-04, Last modification date: 2025-04-09) |
| Primary citation | Diesterbeck, U.S.,Muslinkina, L.A.,Gittis, A.G.,Singh, K.,Moss, B.,Garboczi, D.N. The 2.3 angstrom Structure of A21, a Protein Component of the Conserved Poxvirus Entry-Fusion Complex. J.Mol.Biol., 437:169097-169097, 2025 Cited by PubMed Abstract: Poxviruses are exceptional in having an entry-fusion complex (EFC) consisting of eleven conserved proteins embedded in the membrane of mature virions. With the goal of understanding the function of the EFC, extensive efforts have been made to determine the structures and roles of its components, and to date, structures have been determined for nine of the eleven proteins. Here, we report the crystal structure of A21, the 10 EFC protein, comprising two α-helices clasping a twisted antiparallel β-sheet stabilized by two conserved disulfide bonds. The stability of each of the three A21 loops is provided by hydrogen bonds between main-chain atoms and several highly conserved residues, making the overall fold of A21 and its orthologs resilient to evolutionary change. Based on AlphaFold modeling and phylogenetic analysis of A21, we suggest that its highly conserved N-terminal transmembrane domain and C-terminal α-helix enable A21 integration into EFC, where it primarily interacts with the G3/L5 subcomplex and the smallest of EFC components, the O3 protein. PubMed: 40118206DOI: 10.1016/j.jmb.2025.169097 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report
