7VQQ: Fusion protein of mCerulean and FUS LCD

Cryo-EM structure of amyloid fibril formed by FUS low complexity domain. Determined by electron microscopy at 2.9 Å resolution. Released 22 Dec 2021.

Method: Electron microscopy
Resolution: 2.9 Å
Organisms: Aequorea victoria, Homo sapiens
Chains: 3
Atoms: 1,968
Mol. weight: 155.85 kDa
Released: 22 Dec 2021

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

Secondary structure: helices and β-sheets

7VQQ contains 0 α-helices and 24 β-strands across 3 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: 0 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	55-58	4	1
β-strand	64-65	2	2
β-strand	68-70	3	3
β-strand	73-74	2	4
β-strand	81-82	2	5
β-strand	88	1	6
β-strand	93-96	4	7
β-strand	112	1	8

Chains B and C: 0 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	55-58	4	1
β-strand	62-65	4	2
β-strand	68-70	3	3
β-strand	73-74	2	4
β-strand	81-82	2	5
β-strand	88	1	6
β-strand	93-96	4	7
β-strand	112	1	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
fusion protein of mCerulean and FUS LCD	A, B, C	protein	483	Aequorea victoria, Homo sapiens	P35637 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>7VQQ_1 fusion protein of mCerulean and FUS LCD (chains A, B, C)
MSYYHHHHHHDYDIPTTENLYFQGAMVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGE
GDATYGKLTLKFICTTGKLPVPWPTLVTTLTWGVQCFARYPDHMKQHDFFKSAMPEGYVQ
ERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNAISDNVYITA
DKQKNGIKANFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSKLSKDPNEK
RDHMVLLEFVTAAGITLGMDELYKAGTMDPASNDYTQQATQSYGAYPTQPGQGYSQQSSQ
PYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSY
GQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNP
PQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQ
DRG

Primary citation

Molecular structure of an amyloid fibril formed by FUS low-complexity domain. Sun, Y., Zhang, S., Hu, J. et al. iScience (2022) 25:103701-103701. DOI 10.1016/j.isci.2021.103701 · PubMed

Other PDB entries of the same protein (UniProt P35637 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6KJ3 0.6 Å, 120kV MicroED structure of FUS (37-42) SYSGYS solved from merged datasets at 0.60 A
6KJ1 0.65 Å, 200kV MicroED structure of FUS (37-42) SYSGYS solved from merged datasets at 0.65 A
6KJ4 0.65 Å, 120kV MicroED structure of FUS (37-42) SYSGYS solved from single crystal at 0.65 A
6KJ2 0.67 Å, 200kV MicroED structure of FUS (37-42) SYSGYS solved from single crystal at 0.67 A
5XSG 0.73 Å, Ultrahigh resolution structure of FUS (37-42) SYSGYS determined by MicroED
6BWZ 1.1 Å, SYSGYS from low-complexity domain of FUS, residues 37-42
6BXV 1.1 Å, SYSSYGQS from low-complexity domain of FUS, residues 54-61
6BZP 1.1 Å, STGGYG from low-complexity domain of FUS, residues 77-82
5XRR 1.5 Å, Crystal structure of FUS (54-59) SYSSYG
4FDD 2.3 Å, Crystal structure of KAP beta2-PY-NLS
6XFM 2.62 Å, Molecular structure of the core of amyloid-like fibrils formed by residues 111-214 of FUS
7CYL 2.7 Å, Crystal structure of Karyopherin-beta2 in complex with FUS PY-NLS(P525L)

Browse structure collections

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