8AKW

280 A SynPspA rod after incubation with ATP

これはPDB形式変換不可エントリーです。

8AKW の概要

• エントリーDOI: 10.2210/pdb8akw/pdb
• EMDBエントリー: 15495
• 分子名称: Chloroplast membrane-associated 30 kD protein (1 entity in total)
• 機能のキーワード: nucleotide binding, helical assembly, escrt-iii fold, membrane remodeling, lipid binding protein
• 由来する生物種: Synechocystis sp. PCC 6803
• タンパク質・核酸の鎖数: 60
• 化学式量合計: 1685865.48

構造登録者

Junglas, B.,Hudina, E.,Schoennenbeck, P.,Ritter, I.,Santiago-Schuebel, B.,Huesgen, P.,Sachse, C. (登録日: 2022-07-31, 公開日: 2024-02-14, 最終更新日: 2024-09-04)

主引用文献

Junglas, B.,Hudina, E.,Schonnenbeck, P.,Ritter, I.,Heddier, A.,Santiago-Schubel, B.,Huesgen, P.F.,Schneider, D.,Sachse, C.
Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies.
Nat.Struct.Mol.Biol., 2024

PubMed Abstract: Eukaryotic members of the endosome sorting complex required for transport-III (ESCRT-III) family have been shown to form diverse higher-order assemblies. The bacterial phage shock protein A (PspA) has been identified as a member of the ESCRT-III superfamily, and PspA homo-oligomerizes to form rod-shaped assemblies. As observed for eukaryotic ESCRT-III, PspA forms tubular assemblies of varying diameters. Using electron cryo-electron microscopy, we determined 61 Synechocystis PspA structures and observed in molecular detail how the structural plasticity of PspA rods is mediated by conformational changes at three hinge regions in the monomer and by the fixed and changing molecular contacts between protomers. Moreover, we reduced and increased the structural plasticity of PspA rods by removing the loop connecting helices α3/α4 and the addition of nucleotides, respectively. Based on our analysis of PspA-mediated membrane remodeling, we suggest that the observed mode of structural plasticity is a prerequisite for the biological function of ESCRT-III members.

PubMed: 39152237
DOI: 10.1038/s41594-024-01359-7

実験手法

ELECTRON MICROSCOPY (5.4 Å)