8U0R

The crystal structure of protein A21, a component of the conserved poxvirus entry-fusion complex

8U0R の概要

• エントリーDOI: 10.2210/pdb8u0r/pdb
• 分子名称: Virion membrane protein A21, 2-(2-METHOXYETHOXY)ETHANOL, 2-AMINO-ETHANETHIOL, ... (17 entities in total)
• 機能のキーワード: poxvirus, entry-fusion complex, poxvirus a21 protein, vaccinia virus, viral protein
• 由来する生物種: Vaccinia virus Western Reserve
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 70886.21

構造登録者

Diesterbeck, U.,Gittis, A.G.,Garboczi, D.N.,Moss, B. (登録日: 2023-08-29, 公開日: 2024-09-04, 最終更新日: 2025-04-09)

主引用文献

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

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 10th 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: 40118206
DOI: 10.1016/j.jmb.2025.169097

実験手法

X-RAY DIFFRACTION (2.3 Å)