6YJ5

Focused refinement cryo-EM structure of the yeast mitochondrial complex I sub-stoichiometric sulfur transferase subunit

6YJ5 の概要

• エントリーDOI: 10.2210/pdb6yj5/pdb
• 関連するPDBエントリー: 6YJ4
• EMDBエントリー: 10815 10816
• 分子名称: Rhodanese-like domain-containing protein (1 entity in total)
• 機能のキーワード: nadh:ubiquinone oxidoreductase, sulfur transferase, sub-stoichiometric, complex i, transferase
• 由来する生物種: Yarrowia lipolytica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34661.12

構造登録者

Hirst, J.,Grba, D. (登録日: 2020-04-02, 公開日: 2020-08-12, 最終更新日: 2024-05-22)

主引用文献

Ni, T.,Gerard, S.,Zhao, G.,Dent, K.,Ning, J.,Zhou, J.,Shi, J.,Anderson-Daniels, J.,Li, W.,Jang, S.,Engelman, A.N.,Aiken, C.,Zhang, P.
Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A.
Nat.Struct.Mol.Biol., 27:855-862, 2020

PubMed Abstract: The mature retrovirus capsid consists of a variably curved lattice of capsid protein (CA) hexamers and pentamers. High-resolution structures of the curved assembly, or in complex with host factors, have not been available. By devising cryo-EM methodologies for exceedingly flexible and pleomorphic assemblies, we have determined cryo-EM structures of apo-CA hexamers and in complex with cyclophilin A (CypA) at near-atomic resolutions. The CA hexamers are intrinsically curved, flexible and asymmetric, revealing the capsomere and not the previously touted dimer or trimer interfaces as the key contributor to capsid curvature. CypA recognizes specific geometries of the curved lattice, simultaneously interacting with three CA protomers from adjacent hexamers via two noncanonical interfaces, thus stabilizing the capsid. By determining multiple structures from various helical symmetries, we further revealed the essential plasticity of the CA molecule, which allows formation of continuously curved conical capsids and the mechanism of capsid pattern sensing by CypA.

PubMed: 32747784
DOI: 10.1038/s41594-020-0467-8

実験手法

ELECTRON MICROSCOPY (3.5 Å)