7O1Q: Alpha-hemolysin hybridized Abeta

Amyloid beta oligomer displayed on the alpha hemolysin scaffold. Determined by electron microscopy at 3.4 Å resolution. Released 14 Apr 2021.

Method: Electron microscopy
Resolution: 3.4 Å
Organisms: Staphylococcus aureus, Homo sapiens
Chains: 7
Atoms: 16,513
Mol. weight: 234.21 kDa
Released: 14 Apr 2021

Explore 7O1Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7O1Q contains 21 α-helices and 168 β-strands across 7 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.

Chains A, B, C, D, E, F and G: 3 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	7	1	1
β-strand	14	1	2
β-strand	20-29	10	3
β-strand	34-43	10	3
β-strand	48	1	4
β-strand	51-61	11	3
β-strand	66-70	5	5
β-strand	75-89	15	5
β-strand	97-102	6	3
β-strand	109-127	19	6
β-strand	131-151	21	6
β-strand	153-158	6	5
β-strand	164-171	8	5
β-strand	174-175	2	7
β-strand	181-182	2	7
β-strand	188	1	5
β-strand	192	1	5
β-strand	197	1	8
α-helix	206-208	3
β-strand	210	1	8
α-helix	211-212	2
α-helix	218-221	4
β-strand	224	1	3
β-strand	227-234	8	3
β-strand	242-260	19	5
β-strand	265-285	21	5
β-strand	290-292	3	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-hemolysin hybridized Abeta	A, B, C, D, E, F, G	protein	293	Staphylococcus aureus, Homo sapiens	P05067 (AlphaFold model), Q2G1X0 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G), FASTA

>7O1Q_1 Alpha-hemolysin hybridized Abeta (chains A, B, C, D, E, F, G)
ADSDINIKTGTTDIGSNTTVKTGDLVTYDKENGMHKKVFYSFIDDKNHNKKLLVIRTKGT
IAGQYRVYSEEGANKSGLAWPSAFKVQLQLPDNEVAQISDYYPRNDAEFRHDSGYEVHHQ
KLVFFAEDVGSNKGAIIGLMVGGVVIAYVQPDFKTILESPTDKKVGWKVIFNNMVNQNWG
PYDRDSWNPVYGNQLFMKTRNGSMKAADNFLDPNKASSLLSSGFSPDFATVITMDRKASK
QQTNIDVIYERVRDDYQLHWTSTNWKGTNTKDKWTDRSSERYKIDWEKEEMTN

Primary citation

Cryo-electron Microscopy Imaging of Alzheimer's Amyloid-beta 42 Oligomer Displayed on a Functionally and Structurally Relevant Scaffold. Wu, J., Blum, T.B., Farrell, D.P. et al. Angew Chem Int Ed Engl (2021) 60:18680-18687. DOI 10.1002/anie.202104497 · PubMed

Other PDB entries of the same protein (UniProt P05067 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2FMA 0.85 Å, Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in…
6NB9 1.05 Å, Amyloid-Beta (20-34) with L-isoaspartate 23
6OIZ 1.1 Å, Amyloid-Beta (20-34) wild type
8T82 1.1 Å, Racemic mixture of amyloid beta segment 35-MVGGVV-40 forms heterochiral rippled…
5ONQ 1.17 Å, Alzheimer's Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd-substituted Thermolysin
3JQL 1.2 Å, Crystal Structure of the Complex Formed Between Phospholipase A2 and a Hexapeptide…
3PZZ 1.29 Å, Structure of an amyloid forming peptide GAIIGL (29-34) from amyloid beta
4PQD 1.33 Å, The longer crystal structure of the grow factor like domain from Beta amypoid precusor…
5ONP 1.34 Å, Alzheimer's Amyloid-Beta Peptide Fragment 1-40 in Complex with Cd-substituted Thermolysin
5ONR 1.39 Å, Alzheimer's Amyloid-Beta Peptide Fragment 1-40 in Complex with Thermolysin
4PWQ 1.4 Å, High-resolution crystal structure of the E1-domain of the amyloid precursor protein
7OW1 1.4 Å, Crystal Structure of TAP01 in complex with amyloid beta peptide

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