4V0W
The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)
Summary for 4V0W
| Entry DOI | 10.2210/pdb4v0w/pdb |
| Related | 4V0U 4V0V 4V0X |
| Descriptor | SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT, PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 15B, MANGANESE (II) ION, ... (4 entities in total) |
| Functional Keywords | hydrolase-hydrolase regulator complex, hydrolase/hydrolase regulator |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) More |
| Total number of polymer chains | 4 |
| Total formula weight | 78359.18 |
| Authors | Chen, R.,Yan, Y.,Casado, A.C.,Ron, D.,Read, R.J. (deposition date: 2014-09-18, release date: 2015-03-25, Last modification date: 2024-05-01) |
| Primary citation | Chen, R.,Rato, C.,Yan, Y.,Crespillo-Casado, A.,Clarke, H.J.,Harding, H.P.,Marciniak, S.J.,Read, R.J.,Ron, D. G-actin provides substrate-specificity to eukaryotic initiation factor 2 alpha holophosphatases. Elife, 4:-, 2015 Cited by PubMed Abstract: Dephosphorylation of eukaryotic translation initiation factor 2a (eIF2a) restores protein synthesis at the waning of stress responses and requires a PP1 catalytic subunit and a regulatory subunit, PPP1R15A/GADD34 or PPP1R15B/CReP. Surprisingly, PPP1R15-PP1 binary complexes reconstituted in vitro lacked substrate selectivity. However, selectivity was restored by crude cell lysate or purified G-actin, which joined PPP1R15-PP1 to form a stable ternary complex. In crystal structures of the non-selective PPP1R15B-PP1G complex, the functional core of PPP1R15 made multiple surface contacts with PP1G, but at a distance from the active site, whereas in the substrate-selective ternary complex, actin contributes to one face of a platform encompassing the active site. Computational docking of the N-terminal lobe of eIF2a at this platform placed phosphorylated serine 51 near the active site. Mutagenesis of predicted surface-contacting residues enfeebled dephosphorylation, suggesting that avidity for the substrate plays an important role in imparting specificity on the PPP1R15B-PP1G-actin ternary complex. PubMed: 25774600DOI: 10.7554/eLife.04871 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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