Structural mechanism of trimeric PP2A holoenzyme involving PR70: insight for Cdc6 dephosphorylation

(2S,3S,4E,6E,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid

(3S)-3-methyl-D-aspartic acid; D-METHYL ASPARTIC ACID

Structure of the Ca(2+)-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation.

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct
UNP Q9Y5P8 residues 122-490 and UNP Q99741 residues 70-90

Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha

Medium tumor antigen-associated 61 kDa protein, PP2A subunit A isoform PR65-alpha, PP2A subunit A isoform R1-alpha

PP2A subunit B isoform PR48, Protein phosphatase 2A 48 kDa regulatory subunit

0.1M Na Malonate, 12% PEG 3350 + 6.2mg/mL protein in buffer Tris, 150mM NaCl , pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K

Contains PP2A (C subunit) and LCMT-1 (C subunit methyltransferase)

PP2A Core (Scaffold A subunit + catalytic C subunit bound to inhibitor MCLR)

HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
PP2A A alpha subunit (9-589) , PP2A PR70 B" subunit (122-490) fused at 490 to sequence from CDC6 (70-90) with a 22 amino acid linker derived from JMJD6, PP2A C alpha subunit (FL) , Microcystin-LR (MCLR)
EF Hand, Phosphatase, CDC6 (Substrate), HYDROLASE-TOXIN complex
BINDING SITE FOR CHAIN G OF MICROCYSTIN-LR (MCLR) BOUND FORM
BINDING SITE FOR CHAIN H OF MICROCYSTIN-LR (MCLR) BOUND FORM