6IUG
Cryo-EM structure of the plant actin filaments from Zea mays pollen
Summary for 6IUG
| Entry DOI | 10.2210/pdb6iug/pdb |
| EMDB information | 9734 |
| Descriptor | pollen F-actin, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | microfilament, helix, actin, protein fibril |
| Biological source | Zea mays (Maize) |
| Total number of polymer chains | 5 |
| Total formula weight | 208313.13 |
| Authors | |
| Primary citation | 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 Cited by 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: 31628168DOI: 10.1105/tpc.18.00973 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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