8ETV: Class2 of the INO80-Hexasome complex
Class2 of the INO80-Hexasome complex. Determined by electron microscopy at 3.16 Å resolution. Released 12 Jul 2023.
- Method
- Electron microscopy
- Resolution
- 3.16 Å
- Organisms
- Xenopus laevis, synthetic construct
- Chains
- 8
- Atoms
- 8,682
- Mol. weight
- 221.55 kDa
- Released
- 12 Jul 2023
Explore 8ETV in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8ETV contains 26 α-helices and 14 β-strands across 6 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: 3 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-77 | 13 | |
| β-strand | 84-85 | 2 | 1 |
| α-helix | 87-114 | 28 | |
| β-strand | 119-120 | 2 | 2 |
| α-helix | 122-132 | 11 | |
Chain B: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-29 | 4 | |
| α-helix | 32-42 | 11 | |
| β-strand | 46-47 | 2 | 2 |
| α-helix | 52-76 | 25 | |
| β-strand | 81-82 | 2 | 1 |
| α-helix | 84-94 | 11 | |
Chain C: 6 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 18-22 | 5 | |
| α-helix | 29-37 | 9 | |
| β-strand | 43-44 | 2 | 3 |
| α-helix | 47-73 | 27 | |
| β-strand | 78-79 | 2 | 4 |
| α-helix | 81-90 | 10 | |
| α-helix | 92-97 | 6 | |
| β-strand | 102-103 | 2 | 5 |
| α-helix | 114-116 | 3 | |
Chain D: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 36-46 | 11 | |
| β-strand | 51-52 | 2 | 4 |
| α-helix | 54-81 | 28 | |
| β-strand | 86-87 | 2 | 3 |
| α-helix | 89-99 | 11 | |
| α-helix | 103-120 | 18 | |
Chain E: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 42-43 | 2 | |
| α-helix | 46-57 | 12 | |
| α-helix | 65-79 | 15 | |
| β-strand | 84-85 | 2 | 6 |
| α-helix | 87-114 | 28 | |
| β-strand | 119-120 | 2 | 7 |
| α-helix | 122-132 | 11 | |
Chain F: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-29 | 3 | |
| α-helix | 32-41 | 10 | |
| β-strand | 46-47 | 2 | 7 |
| α-helix | 51-77 | 27 | |
| β-strand | 81-82 | 2 | 6 |
| α-helix | 84-93 | 10 | |
| β-strand | 98-99 | 2 | 5 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone H3.2 | A, E | protein | 136 | Xenopus laevis | P02302 (AlphaFold model), P84233 (AlphaFold model) |
| Histone H4 | B, F | protein | 103 | Xenopus laevis | P62799 (AlphaFold model) |
| Histone H2A type 1 | C | protein | 130 | Xenopus laevis | Q6AZJ8 (AlphaFold model) |
| Histone H2B 1.1 | D | protein | 123 | Xenopus laevis | P02281 |
| DNA (110-mer) | I | DNA | 227 | synthetic construct | |
| DNA (110-mer) | J | DNA | 227 | synthetic construct | |
Sequence of entity 1 (A, E), FASTA
>8ETV_1 Histone H3.2 (chains A, E)
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTE
LLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLAAIHAKRVTI
MPKDIQLARRIRGERA
Sequence of entity 2 (B, F), FASTA
>8ETV_2 Histone H4 (chains B, F)
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK
VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 3 (C), FASTA
>8ETV_3 Histone H2A type 1 (chains C)
MSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT
AEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKK
TESSKSAKSK
Sequence of entity 4 (D), FASTA
>8ETV_4 Histone H2B 1.1 (chains D)
MAKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIM
NSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYT
SAK
Sequence of entity 5 (I), FASTA
>8ETV_5 DNA (110-MER) (chains I)
CTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAA
ACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCA
GGCACGTGTCAGATATATACATCCTGTGCATGTATTGAACAGCGACCTTGCCGGTGCCAG
TCGGATAGTGTTCCGAGCTCCCACTCTAGAGGATCCCCGGGTACCGA
Sequence of entity 6 (J), FASTA
>8ETV_6 DNA (110-MER) (chains J)
TCGGTACCCGGGGATCCTCTAGAGTGGGAGCTCGGAACACTATCCGACTGGCACCGGCAA
GGTCGCTGTTCAATACATGCACAGGATGTATATATCTGACACGTGCCTGGAGACTAGGGA
GTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTA
GAGCTGTCTACGACCAATTGAGCGGCCTCGGCACCGGGATTCTCCAG
Primary citation
Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility. Wu, H., Munoz, E.N., Hsieh, L.J. et al. Science (2023) 381:319-324. DOI 10.1126/science.adf4197 · PubMed
Other PDB entries of the same protein (UniProt P02302 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1M19 2.3 Å, Ligand binding alters the structure and dynamics of nucleosomal DNA
- 6YN1 2.35 Å, Crystal structure of histone chaperone APLF acidic domain bound to the histone…
- 1M18 2.45 Å, Ligand binding alters the structure and dynamics of nucleosomal DNA
- 1M1A 2.65 Å, Ligand binding alters the structure and dynamics of nucleosomal DNA
- 1AOI 2.8 Å, Complex between nucleosome core particle (H3,H4,H2A,H2B) and 146 bp long DNA fragment
- 8TOF 2.8 Å, Rpd3S bound to an H3K36Cme3 modified nucleosome
- 8U5H 3.23 Å, Cryo-EM structure of human DNMT3A UDR bound to H2AK119ub1-modified nucleosome
- 6PX1 3.3 Å, Set2 bound to nucleosome
- 8DU4 3.55 Å, Complex between RbBP5-WDR5 and an H2B-ubiquitinated nucleosome
- 7M1X 3.7 Å, Cryo-EM Structure of Nucleosome containing mouse histone variant H2A.Z
- 6NZO 3.8 Å, Set2 bound to nucleosome
- 6PX3 4.1 Å, Set2 bound to nucleosome
Browse structure collections
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