Molecular architecture of the glycogen- committed PP1/PTG holoenzyme.

Semrau MS, Giachin G, Covaceuszach S, Cassetta A, Demitri N, Storici P, Lolli G
Nat Commun 13(1):6199 (2022 Oct 19)
PMID: 36261419
doi: 10.1038/s41467-022-33693-z 		Submitted to SASBDB: 2021 Dec 9
Published in SASBDB:

SASDNF2 – Serine/threonine-protein phosphatase (PP1) bound to Protein phosphatase 1 (PTG)

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitProtein phosphatase 1 regulatory subunit 3C experimental SAS data
DAMMIF model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 37 kDa Homo sapiens protein
Protein phosphatase 1 regulatory subunit 3C monomer, 23 kDa Homo sapiens protein
Buffer: 50 mM Tris pH 8.0, 0.5 M NaCl, 10% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 7
RgGuinier 3.3 nm
Dmax 11.9 nm
VolumePorod 87 nm3

SASDNG2 – Serine/threonine-protein phosphatase (PP1) bound to Protein phosphatase 1 (PTG) and cyclodextrin

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitProtein phosphatase 1 regulatory subunit 3C experimental SAS data
DAMFILT model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 37 kDa Homo sapiens protein
Protein phosphatase 1 regulatory subunit 3C monomer, 23 kDa Homo sapiens protein
Buffer: 50 mM Tris pH 8.0, 0.5 M NaCl, 10% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 7
RgGuinier 3.6 nm
Dmax 12.3 nm
VolumePorod 89 nm3