8TK7
Myxococcus xanthus EncA protein shell with compartmentalized SNAP-tag cargo protein
8TK7 の概要
| エントリーDOI | 10.2210/pdb8tk7/pdb |
| EMDBエントリー | 41322 |
| 分子名称 | Type 1 encapsulin shell protein EncA, Methylated-DNA--protein-cysteine methyltransferase (2 entities in total) |
| 機能のキーワード | encapsulin, nanocompartment, virus like particle |
| 由来する生物種 | Myxococcus xanthus DK 1622 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 159523.73 |
| 構造登録者 | |
| 主引用文献 | Kwon, S.,Andreas, M.P.,Giessen, T.W. Structure and heterogeneity of a highly cargo-loaded encapsulin shell. J.Struct.Biol., 215:108022-108022, 2023 Cited by PubMed Abstract: Encapsulins are self-assembling protein nanocompartments able to selectively encapsulate dedicated cargo enzymes. Encapsulins are widespread across bacterial and archaeal phyla and are involved in oxidative stress resistance, iron storage, and sulfur metabolism. Encapsulin shells exhibit icosahedral geometry and consist of 60, 180, or 240 identical protein subunits. Cargo encapsulation is mediated by the specific interaction of targeting peptides or domains, found in all cargo proteins, with the interior surface of the encapsulin shell during shell self-assembly. Here, we report the 2.53 Å cryo-EM structure of a heterologously produced and highly cargo-loaded T3 encapsulin shell from Myxococcus xanthus and explore the systems' structural heterogeneity. We find that exceedingly high cargo loading results in the formation of substantial amounts of distorted and aberrant shells, likely caused by a combination of unfavorable steric clashes of cargo proteins and shell conformational changes. Based on our cryo-EM structure, we determine and analyze the targeting peptide-shell binding mode. We find that both ionic and hydrophobic interactions mediate targeting peptide binding. Our results will guide future attempts at rationally engineering encapsulins for biomedical and biotechnological applications. PubMed: 37657675DOI: 10.1016/j.jsb.2023.108022 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.53 Å) |
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