8SO0: PP2A:B55-FAM122A complex

Cryo-EM structure of the PP2A:B55-FAM122A complex. Determined by electron microscopy at 2.8 Å resolution. Released 25 Oct 2023.

Method: Electron microscopy
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,756
Mol. weight: 163.71 kDa
Ligands: FE, ZN
Released: 25 Oct 2023

Explore 8SO0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8SO0 contains 88 α-helices and 53 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 58 helices, 0 β-strands

Element	Residues	Length
α-helix	11-19	9
α-helix	25-33	9
α-helix	35-42	8
α-helix	44-46	3
α-helix	47-51	5
α-helix	52-56	5
α-helix	63-73	11
α-helix	83-89	7
α-helix	90-96	7
α-helix	102-116	15
α-helix	121-123	3
α-helix	124-128	5
α-helix	129-136	8
α-helix	141-147	7
α-helix	148-150	3
α-helix	151-154	4
α-helix	160-174	15
α-helix	179-195	17
α-helix	198-200	3
α-helix	201-205	5
α-helix	206-213	8
α-helix	218-234	17
α-helix	237-243	7
α-helix	245-252	8
α-helix	257-265	9
α-helix	267-274	8
α-helix	276-278	3
α-helix	279-283	5
α-helix	284-291	8
α-helix	296-304	9
α-helix	306-312	7
α-helix	318-321	4
α-helix	322-326	5
α-helix	327-334	8
α-helix	339-349	11
α-helix	350-352	3
α-helix	353-360	8
α-helix	361-365	5
α-helix	366-373	8
α-helix	378-386	9
α-helix	389-395	7
α-helix	398-412	15
α-helix	417-434	18
α-helix	436-438	3
α-helix	439-443	5
α-helix	444-451	8
α-helix	456-477	22
α-helix	478-482	5
α-helix	483-486	4
α-helix	487-491	5
α-helix	495-516	22
α-helix	517-521	5
α-helix	522-528	7
α-helix	534-547	14
α-helix	553-555	3
α-helix	556-560	5
α-helix	561-568	8
α-helix	573-586	14

Chain B: 12 helices, 38 β-strands

Element	Residues	Length	Sheet
β-strand	12-19	8	1
α-helix	27-29	3
β-strand	31-36	6	2
β-strand	42-47	6	2
β-strand	51-57	7	2
α-helix	69-70	2
β-strand	71-78	8	2
β-strand	83-85	3	3
β-strand	90-92	3	3
β-strand	98-101	4	4
α-helix	102-103	2
β-strand	109-114	6	4
β-strand	119-132	14	4
β-strand	137	1	5
β-strand	143	1	5
α-helix	146-148	3
β-strand	156-172	17	4
β-strand	182-185	4	6
β-strand	191-195	5	6
β-strand	199-204	6	6
β-strand	207-216	10	6
α-helix	222-224	3
β-strand	229-234	6	7
β-strand	241-246	6	7
β-strand	251-255	5	7
β-strand	267-269	3	7
α-helix	282-285	4
β-strand	290-293	4	8
β-strand	299-303	5	8
β-strand	307-312	6	8
β-strand	321-324	4	8
α-helix	327-332	6
α-helix	333-338	6
α-helix	341-343	3
β-strand	348-350	3	9
β-strand	356-360	5	9
β-strand	362	1	10
β-strand	365-370	6	9
β-strand	375-380	6	9
α-helix	383-385	3
β-strand	390-391	2	1
α-helix	392-394	3
β-strand	395	1	9
β-strand	397-398	2	11
β-strand	408-409	2	11
α-helix	410-412	3
β-strand	418	1	10
β-strand	421-424	4	1
β-strand	430-434	5	1
β-strand	438-444	7	1

Chain C: 16 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	3-18	16
α-helix	22-24	3
α-helix	25-39	15
β-strand	45-48	4	12
β-strand	52-55	4	13
α-helix	62-72	11
β-strand	80-82	3	13
α-helix	93-106	14
β-strand	111-113	3	13
α-helix	121-126	6
α-helix	129-137	9
α-helix	141-150	10
β-strand	156-159	4	12
β-strand	163-166	4	12
α-helix	177-181	5
α-helix	194-200	7
β-strand	202-203	2	14
β-strand	209-211	3	14
β-strand	218-220	3	14
α-helix	222-232	11
β-strand	236-239	4	12
β-strand	248-251	4	12
β-strand	256-259	4	12
α-helix	265-267	3
α-helix	271-272	2
β-strand	273-278	6	13
α-helix	279	1
β-strand	284-289	6	13
α-helix	290-292	3
β-strand	300-301	2	6
α-helix	304-305	2

Chain D: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	84-93	10
α-helix	98-110	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform	A	protein	584	Homo sapiens	P30153 (AlphaFold model)
Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform	B	protein	451	Homo sapiens	P63151 (AlphaFold model)
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform	C	protein	311	Homo sapiens	P67775 (AlphaFold model)
PPP2R1A-PPP2R2A-interacting phosphatase regulator 1	D	protein	95	Homo sapiens	Q96E09 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8SO0_1 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (chains A)
GHMSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEV
LLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLE
AHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAA
ASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVM
PTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHK
VKEFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDNTIEHL
LPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIE
YMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPK
VLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQ
KIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA

Sequence of entity 2 (B), FASTA

>8SO0_2 Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (chains B)
GHMGSAGAGGGNDIQWCFSQVKGAVDDDVAEADIISTVEFNHSGELLATGDKGGRVVIFQ
QEQENKIQSHSRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQKNAAQFLLSTND
KTIKLWKISERDKRPEGYNLKEEDGRYRDPTTVTTLRVPVFRPMDLMVEASPRRIFANAH
TYHINSISINSDYETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAEFHP
NSCNTFVYSSSKGTIRLCDMRASALCDRHSKLFEEPEDPSNRSFFSEIISSISDVKFSHS
GRYMMTRDYLSVKIWDLNMENRPVETYQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSV
VMTGSYNNFFRMFDRNTKRDITLEASRENNKPRTVLKPRKVCASGKRKKDEISVDSLDFN
KKILHTAWHPKENIIAVATTNNLYIFQDKVN

Sequence of entity 3 (C), FASTA

>8SO0_3 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C)
GHMDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDV
HGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNH
ESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLD
HIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVS
RAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEP
HVTRRTPDYFL

Sequence of entity 4 (D), FASTA

>8SO0_4 PPP2R1A-PPP2R2A-interacting phosphatase regulator 1 (chains D)
GHMGGGLRRSNSAPLIHGLSDSSPVFQDEAPSARRNRTTFPSRHGLLLPASPVRMHSSRL
HQIKQEEGMDLINRETVHEREVQTAMQISHSWEES

Ligands and cofactors

ID	Name	Formula	Copies
FE	FE (III) ion	Fe	1
ZN	Zinc ion	Zn	1

Primary citation

Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. Padi, S.K.R., Vos, M.R., Godek, R.J. et al. Nature (2024) 625:195-203. DOI 10.1038/s41586-023-06870-3 · PubMed

Other PDB entries of the same protein (UniProt P30153 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1B3U 2.3 Å, Crystal structure of constant regulatory domain of human PP2A, PR65ALPHA
4I5L 2.43 Å, Structural mechanism of trimeric PP2A holoenzyme involving PR70: insight for Cdc6…
8TWE 2.55 Å, Cryo-EM structure of the PP2A:B55-FAM122A complex, B55 body
2IE4 2.6 Å, Structure of the Protein Phosphatase 2A Core Enzyme Bound to okadaic acid
9C6B 2.6 Å, PP2A:B55-p107 substrate complex
8TWI 2.69 Å, Cryo-EM structure of the PP2A:B55-FAM122A complex, PP2Ac body
8U1X 2.7 Å, The structure of the PP2A-B56Delta holoenzyme mutant - E197K
9C7T 2.7 Å, PP2A:B55-Eya3 substrate complex
8TTB 2.77 Å, Cryo-EM structure of the PP2A:B55-ARPP19 complex
2IE3 2.8 Å, Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor-inducing Toxins
3C5W 2.8 Å, Complex between PP2A-specific methylesterase PME-1 and PP2A core enzyme
4I5N 2.8 Å, Structural mechanism of trimeric PP2A holoenzyme involving PR70: insight for Cdc6…

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