8S7E: SKP1-FBXO22

Name: PDB 8S7E: Cryo-EM structure of SKP1-FBXO22
Published: 2024-12-11
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Cryo-EM structure of SKP1-FBXO22. Determined by electron microscopy at 3.4 Å resolution. Released 11 Dec 2024.

Method: Electron microscopy
Resolution: 3.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,664
Mol. weight: 62.15 kDa
Released: 11 Dec 2024

Explore 8S7E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8S7E contains 22 α-helices and 22 β-strands across 2 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	18-23	6
α-helix	25-32	8
α-helix	52-65	14
α-helix	68-70	3
α-helix	87-93	7
α-helix	97-110	14
α-helix	113-127	15
α-helix	132-138	7
α-helix	147-156	10
α-helix	158-161	4

Chain B: 12 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	27-35	9
α-helix	39-46	8
α-helix	50-61	12
β-strand	67	1	1
α-helix	83-91	9
β-strand	99-104	6	1
β-strand	105-107	3	2
α-helix	131-138	8
β-strand	144-145	2	1
β-strand	148-150	3	2
β-strand	152-155	4	3
α-helix	164-165	2
β-strand	166-168	3	3
β-strand	176-180	5	1
β-strand	182	1	4
β-strand	185	1	4
β-strand	188-192	5	5
α-helix	203-208	6
β-strand	217-225	9	5
α-helix	236-244	9
β-strand	249-255	7	5
β-strand	257-258	2	2
β-strand	275-281	7	5
β-strand	286-291	6	3
α-helix	299-311	13
β-strand	319-326	8	3
α-helix	332-334	3
α-helix	340-348	9
α-helix	352-353	2
β-strand	354-359	6	3
β-strand	362-363	2	5
β-strand	368-370	3	3
β-strand	387-388	2	5
β-strand	392-398	7	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
S-phase kinase-associated protein 1	A	protein	162	Homo sapiens	P63208 (AlphaFold model)
F-box only protein 22	B	protein	395	Homo sapiens	Q8NEZ5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8S7E_1 S-phase kinase-associated protein 1 (chains A)
PSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQW
CTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTCK
TVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK

Sequence of entity 2 (B), FASTA

>8S7E_2 F-box only protein 22 (chains B)
GGSGSSVDPRSTFVLSNLAEVVERVLTFLPAKALLRVACVCRLWRECVRRVLRTHRSVTW
ISAGLAEAGHLEGHCLVRVVAEELENVRILPHTVLYMADSETFISLEECRGHKRARKRTS
METALALEKLFPKQCQVLGIVTPGIVVTPMGSGSNRPQEIEIGESGFALLFPQIEGIKIQ
PFHFIKDPKNLTLERHQLTEVGLLDNPELRVVLVFGYNCCKVGASNYLQQVVSTFSDMNI
ILAGGQVDNLSSLTSEKNPLDIDASGVVGLSFSGHRIQSATVLLNEDVSDEKTAEAAMQR
LKAANIPEHNTIGFMFACVGRGFQYYRAKGNVEADAFRKFFPSVPLFGFFGNGEIGCDRI
VTGNFILRKCNEVKDDDLFHSYTTIMALIHLGSSK

Primary citation

Dual BACH1 regulation by complementary SCF-type E3 ligases. Goretzki, B., Khoshouei, M., Schroder, M. et al. Cell (2024) 187:7585-7602.e25. DOI 10.1016/j.cell.2024.11.006 · PubMed

Other PDB entries of the same protein (UniProt P63208 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1FS1 1.8 Å, Insights into scf ubiquitin ligases from the structure of the SKP1-SKP2 complex
6M90 2.05 Å, Monophosphorylated pSer33 b-Catenin peptide, b-TrCP/Skp1, NRX-2776 ternary complex
2AST 2.3 Å, Crystal structure of Skp1-Skp2-Cks1 in complex with a p27 peptide
6M92 2.35 Å, Monophosphorylated pSer33 b-Catenin peptide, b-TrCP/Skp1, NRX-2663 ternary complex
2E31 2.4 Å, Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase
6M91 2.4 Å, Monophosphorylated pSer33 b-Catenin peptide, b-TrCP/Skp1, NRX-103094 ternary complex
2OVR 2.5 Å, Structure of the Skp1-Fbw7-CyclinEdegN complex
6M93 2.5 Å, Monophosphorylated pSer33 b-Catenin peptide, b-TrCP/Skp1, NRX-1933 ternary complex
6WNX 2.5 Å, FBXW11-SKP1 in complex with a pSer33/pSer37 Beta-Catenin peptide
5IBK 2.5 Å, Skp1-F-box in complex with a ubiquitin variant
6O60 2.5 Å, Crystal structure of GGTase3-FBXL2-SKP1 complex
5JH5 2.55 Å, Structural Basis for the Hierarchical Assembly of the Core of PRC1.1

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