7A08: CGAS Nucleosome complex
CryoEM Structure of cGAS Nucleosome complex. Determined by electron microscopy at 3.11 Å resolution. Released 23 Sept 2020.
- Method
- Electron microscopy
- Resolution
- 3.11 Å
- Organisms
- Mus musculus, synthetic construct, Homo sapiens
- Chains
- 11
- Atoms
- 13,969
- Mol. weight
- 242.82 kDa
- Ligands
- ZN
- Released
- 23 Sept 2020
Explore 7A08 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7A08 contains 50 α-helices and 34 β-strands across 9 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: 15 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 149-184 | 36 | |
| β-strand | 193-194 | 2 | 1 |
| β-strand | 211 | 1 | 1 |
| β-strand | 214-219 | 6 | 1 |
| β-strand | 223-226 | 4 | 2 |
| β-strand | 235 | 1 | 1 |
| β-strand | 236-239 | 4 | 2 |
| β-strand | 252 | 1 | 2 |
| β-strand | 257 | 1 | 2 |
| α-helix | 258 | 1 | |
| α-helix | 259-276 | 18 | |
| α-helix | 285-287 | 3 | |
| β-strand | 294-298 | 5 | 1 |
| β-strand | 304-314 | 11 | 1 |
| α-helix | 317-319 | 3 | |
| α-helix | 320-322 | 3 | |
| α-helix | 329-332 | 4 | |
| α-helix | 334-338 | 5 | |
| β-strand | 345-349 | 5 | 1 |
| β-strand | 363-366 | 4 | 1 |
| α-helix | 368-376 | 9 | |
| α-helix | 395-411 | 17 | |
| α-helix | 414-417 | 4 | |
| α-helix | 421-431 | 11 | |
| α-helix | 445-462 | 18 | |
| β-strand | 466 | 1 | 3 |
| β-strand | 474 | 1 | 3 |
| α-helix | 483-497 | 15 | |
| α-helix | 502-504 | 3 | |
Chain b: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-20 | 4 | |
| α-helix | 27-36 | 10 | |
| β-strand | 43 | 1 | 4 |
| α-helix | 47-72 | 26 | |
| β-strand | 77-78 | 2 | 5 |
| α-helix | 91-96 | 6 | |
| β-strand | 100-102 | 3 | 6 |
Chain c: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 38-47 | 10 | |
| β-strand | 53-54 | 2 | 5 |
| α-helix | 58-83 | 26 | |
| β-strand | 89 | 1 | 4 |
| α-helix | 91-101 | 11 | |
| α-helix | 105-114 | 10 | |
| α-helix | 116-122 | 7 | |
Chain d: 6 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 41-42 | 2 | |
| α-helix | 45-49 | 5 | |
| α-helix | 51-54 | 4 | |
| α-helix | 64-75 | 12 | |
| β-strand | 83-84 | 2 | 7 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 8 |
| α-helix | 121-130 | 10 | |
Chain e: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 31-41 | 11 | |
| β-strand | 45-46 | 2 | 9 |
| α-helix | 51-75 | 25 | |
| β-strand | 80-81 | 2 | 10 |
| α-helix | 83-93 | 11 | |
| β-strand | 96-98 | 3 | 11 |
Chain f: 5 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-21 | 5 | |
| α-helix | 27-35 | 9 | |
| β-strand | 42-43 | 2 | 12 |
| α-helix | 47-73 | 27 | |
| β-strand | 77-78 | 2 | 13 |
| α-helix | 80-89 | 10 | |
| α-helix | 93-96 | 4 | |
| β-strand | 100-102 | 3 | 11 |
Chain g: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 40-48 | 9 | |
| β-strand | 53-54 | 2 | 13 |
| α-helix | 56-83 | 28 | |
| β-strand | 88-89 | 2 | 12 |
| α-helix | 91-101 | 11 | |
| α-helix | 105-121 | 17 | |
Chain h: 3 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 64-75 | 12 | |
| β-strand | 83-84 | 2 | 10 |
| α-helix | 87-112 | 26 | |
| β-strand | 118-119 | 2 | 9 |
| α-helix | 125-129 | 5 | |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Cyclic GMP-AMP synthase | a | protein | 370 | Mus musculus | Q8C6L5 (AlphaFold model) |
| Nucleosomal DNA strand 1 | I | DNA | 147 | synthetic construct | |
| Nucleosomal DNA strand 2 | J | DNA | 147 | synthetic construct | |
| Histone H2A type 1-C | b, f | protein | 129 | Homo sapiens | Q93077 (AlphaFold model) |
| Histone H2B type 1-C/E/F/G/I | c, g | protein | 125 | Homo sapiens | P62807 (AlphaFold model) |
| Histone H3.3 | d, h | protein | 135 | Homo sapiens | P84243 (AlphaFold model) |
| Histone H4 | e, i | protein | 102 | Homo sapiens | P62805 |
Sequence of entity 1 (a), FASTA
>7A08_1 Cyclic GMP-AMP synthase (chains a)
GAMRGSRKEPDKLKKVLDKLRLKRKDISEAAETVNKVVERLLRRMQKRESEFKGVEQLNT
GSYYEHVKISAPNEFDVMFKLEVPRIELQEYYETGAFYLVKFKRIPRGNPLSHFLEGEVL
SATKMLSKFRKIIKEEVKEIKDIDVSVEKEKPGSPAVTLLIRNPEEISVDIILALESKGS
WPISTKEGLPIQGWLGTKVRTNLRREPFYLVPKNAKDGNSFQGETWRLSFSHTEKYILNN
HGIEKTCCESSGAKCCRKECLKLMKYLLEQLKKEFQELDAFCSYHVKTAIFHMWTQDPQD
SQWDPRNLSSCFDKLLAFFLECLRTEKLDHYFIPKFNLFSQELIDRKSKEFLSKKIEYER
NNGFPIFDKL
Sequence of entity 2 (I), FASTA
>7A08_2 Nucleosomal DNA strand 1 (chains I)
CTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGCAAGCTCTAGCACCGCTTAA
ACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCA
GGCACGTGTCAGATATATACATCCTGT
Sequence of entity 3 (J), FASTA
>7A08_3 Nucleosomal DNA strand 2 (chains J)
ACAGGATGTATATATCTGACACGTGCCTGGAGACTAGGGAGTAATCCCCTTGGCGGTTAA
AACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTTGCTACGACCAATTG
AGCGGCCTCGGCACCGGGATTCTCCAG
Sequence of entity 4 (b, f), FASTA
>7A08_4 Histone H2A type 1-C (chains b, f)
SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKT
ESHHKAKGK
Sequence of entity 5 (c, g), FASTA
>7A08_5 Histone H2B type 1-C/E/F/G/I (chains c, g)
PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMG
IMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTK
YTSSK
Sequence of entity 6 (d, h), FASTA
>7A08_6 Histone H3.3 (chains d, h)
ARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 7 (e, i), FASTA
>7A08_7 Histone H4 (chains e, i)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 1 |
Primary citation
Structural basis for sequestration and autoinhibition of cGAS by chromatin. Michalski, S., de Oliveira Mann, C.C., Stafford, C.A. et al. Nature (2020) 587:678-682. DOI 10.1038/s41586-020-2748-0 · PubMed
Other PDB entries of the same protein (UniProt Q8C6L5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8SHK 1.71 Å, Structure of binary complex of mouse cGAS and bound ATP
- 8SHU 1.71 Å, Structure of mouse cGAS
- 8SHY 1.77 Å, Structure of binary complex of mouse cGAS QN and bound ATP
- 5XZG 1.83 Å, Mouse cGAS bound to the inhibitor RU521
- 4O6A 1.86 Å, Mouse cyclic GMP-AMP synthase (cGAS) in complex with DNA
- 4K98 1.94 Å, Structure of Ternary Complex of cGAS with dsDNA and Bound 5 -pppG(2 ,5 )pG
- 4K99 1.95 Å, Structure of Ternary Complex of cGAS with dsDNA and Bound 5 -pppdG(2 ,5 )pdG
- 4K8V 2.0 Å, Structure of cyclic GMP-AMP Synthase (cGAS)
- 7UTT 2.04 Å, Structure of Non-hydrolyzable ATP (ApCpp) binds to Cyclic GMP AMP synthase (cGAS)…
- 4K96 2.08 Å, Structure of Binary Complex of cGAS with Bound dsDNA
- 5XZB 2.13 Å, Mouse cGAS bound to the inhibitor RU365
- 7BUJ 2.13 Å, mcGAS bound with pppGpG
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