6YW7
Cryo-EM structure of the ARP2/3 1A5C isoform complex.
Summary for 6YW7
| Entry DOI | 10.2210/pdb6yw7/pdb |
| EMDB information | 10960 |
| Descriptor | Actin-related protein 3, Actin-related protein 2/3 complex subunit 2, Actin-related protein 2/3 complex subunit 3, ... (8 entities in total) |
| Functional Keywords | cytoskeleton, structural protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 7 |
| Total formula weight | 225882.53 |
| Authors | von Loeffelholz, O.,Moores, C.,Purkiss, A. (deposition date: 2020-04-29, release date: 2020-07-22, Last modification date: 2024-05-22) |
| Primary citation | von Loeffelholz, O.,Purkiss, A.,Cao, L.,Kjaer, S.,Kogata, N.,Romet-Lemonne, G.,Way, M.,Moores, C.A. Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms. Biol Open, 9:-, 2020 Cited by PubMed Abstract: The Arp2/3 complex regulates many cellular processes by stimulating formation of branched actin filament networks. Because three of its seven subunits exist as two different isoforms, mammals produce a family of Arp2/3 complexes with different properties that may be suited to different physiological contexts. To shed light on how isoform diversification affects Arp2/3 function, we determined a 4.2 Å resolution cryo-EM structure of the most active human Arp2/3 complex containing ARPC1B and ARPC5L, and compared it with the structure of the least active ARPC1A-ARPC5-containing complex. The architecture of each isoform-specific Arp2/3 complex is the same. Strikingly, however, the N-terminal half of ARPC5L is partially disordered compared to ARPC5, suggesting that this region of ARPC5/ARPC5L is an important determinant of complex activity. Confirming this idea, the nucleation activity of Arp2/3 complexes containing hybrid ARPC5/ARPC5L subunits is higher when the ARPC5L N-terminus is present, thereby providing insight into activity differences between the different Arp2/3 complexes. PubMed: 32661131DOI: 10.1242/bio.054304 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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