6IUG

Cryo-EM structure of the plant actin filaments from Zea mays pollen

6IUG の概要

• エントリーDOI: 10.2210/pdb6iug/pdb
• EMDBエントリー: 9734
• 分子名称: pollen F-actin, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: microfilament, helix, actin, protein fibril
• 由来する生物種: Zea mays (Maize)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 208313.13

構造登録者

Ren, Z.H.,Zhang, Y.,Zhang, Y.,He, Y.Q.,Du, P.Z.,Wang, Z.X.,Sun, F.,Ren, H.Y. (登録日: 2018-11-28, 公開日: 2019-11-06, 最終更新日: 2024-03-27)

主引用文献

Ren, Z.,Zhang, Y.,Zhang, Y.,He, Y.,Du, P.,Wang, Z.,Sun, F.,Ren, H.
Cryo-EM Structure of Actin Filaments fromZea maysPollen.
Plant Cell, 31:2855-2867, 2019

PubMed Abstract: Actins are among the most abundant and conserved proteins in eukaryotic cells, where they form filamentous structures that perform vital roles in key cellular processes. Although large amounts of data on the biochemical activities, dynamic behaviors, and important cellular functions of plant actin filaments have accumulated, their structural basis remains elusive. Here, we report a 3.9 Å structure of the plant actin filament from pollen (ZMPA) using cryo-electron microscopy. The structure shows a right-handed, double-stranded (two parallel strands) and staggered architecture that is stabilized by intra- and interstrand interactions. While the overall structure resembles that of other actin filaments, its DNase I binding loop bends farther outward, adopting an open conformation similar to that of the jasplakinolide- or beryllium fluoride (BeF)-stabilized rabbit skeletal muscle actin (RSMA) filament. Single-molecule magnetic tweezers analysis revealed that the ZMPA filament can resist a greater stretching force than the RSMA filament. Overall, these data provide evidence that plant actin filaments have greater stability than animal actin filaments, which might be important to their role as tracks for long-distance vesicle and organelle transportation.plantcell;31/12/2855/FX1F1fx1.

PubMed: 31628168
DOI: 10.1105/tpc.18.00973

実験手法

ELECTRON MICROSCOPY (3.9 Å)