8QTT: 14-3-3-like protein GF14 omega

Crystal structure of a C-terminally truncated version of Arabidopsis thaliana 14-3-3 omega in complex with a phosphopeptide from the inhibitor protein BKI1. Determined by X-ray diffraction at 2.35 Å resolution. Released 15 Nov 2023.

Method: X-ray diffraction
Resolution: 2.35 Å
Organism: Arabidopsis thaliana
Chains: 20
Atoms: 19,572
Mol. weight: 279.34 kDa
Released: 15 Nov 2023

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

Secondary structure: helices and β-sheets

8QTT contains 137 α-helices and 0 β-strands across 10 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: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-34	14
α-helix	39-41	3
α-helix	42-75	34
α-helix	79-106	28
α-helix	107-111	5
α-helix	112-114	3
α-helix	118-138	21
α-helix	141-165	25
α-helix	171-182	12
α-helix	183-187	5
α-helix	191-207	17
α-helix	209-211	3
α-helix	216-235	20

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-34	14
α-helix	39-41	3
α-helix	42-76	35
α-helix	79-106	28
α-helix	107-111	5
α-helix	112-114	3
α-helix	118-138	21
α-helix	141-165	25
α-helix	171-182	12
α-helix	183-187	5
α-helix	191-209	19
α-helix	218-235	18

Chain C: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-34	14
α-helix	39-41	3
α-helix	42-76	35
α-helix	79-106	28
α-helix	107-111	5
α-helix	112-114	3
α-helix	118-138	21
α-helix	141-165	25
α-helix	171-182	12
α-helix	183-187	5
α-helix	191-206	16
α-helix	209-211	3
α-helix	215-233	19

Chain D: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-34	14
α-helix	39-41	3
α-helix	42-75	34
α-helix	79-106	28
α-helix	107-111	5
α-helix	112-114	3
α-helix	118-136	19
α-helix	141-165	25
α-helix	171-182	12
α-helix	183-187	5
α-helix	191-207	17
α-helix	209-211	3
α-helix	215-235	21

Chain E: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-34	14
α-helix	39-41	3
α-helix	42-76	35
α-helix	79-106	28
α-helix	107-111	5
α-helix	112-114	3
α-helix	118-138	21
α-helix	141-165	25
α-helix	171-182	12
α-helix	183-187	5
α-helix	191-207	17
α-helix	209-211	3
α-helix	215-234	20

Chain F: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-34	14
α-helix	39-41	3
α-helix	42-76	35
α-helix	79-106	28
α-helix	107-111	5
α-helix	112-114	3
α-helix	118-136	19
α-helix	141-165	25
α-helix	171-182	12
α-helix	183-187	5
α-helix	191-207	17
α-helix	217-235	19

Chains G and J: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-34	14
α-helix	39-41	3
α-helix	42-76	35
α-helix	79-106	28
α-helix	107-111	5
α-helix	112-114	3
α-helix	118-138	21
α-helix	141-165	25
α-helix	171-182	12
α-helix	183-187	5
α-helix	191-207	17
α-helix	209-211	3
α-helix	215-235	21

Chain H: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	5-18	14
α-helix	21-34	14
α-helix	39-41	3
α-helix	42-76	35
α-helix	79-106	28
α-helix	107-111	5
α-helix	112-114	3
α-helix	118-138	21
α-helix	141-165	25
α-helix	171-182	12
α-helix	183-187	5
α-helix	191-206	16
α-helix	218-235	18

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
14-3-3-like protein GF14 omega	A, B, C, D, E, F, G, H, I, J	protein	241	Arabidopsis thaliana	Q01525 (AlphaFold model)
BRI1 kinase inhibitor 1	K, L, M, N, O, P, Q, R, S, T	protein	6	Arabidopsis thaliana

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

>8QTT_1 14-3-3-like protein GF14 omega (chains A, B, C, D, E, F, G, H, I, J)
AGMASGREEFVYMAKLAEQAERYEEMVEFMEKVSAAVDGDELTVEERNLLSVAYKNVIGA
RRASWRIISSIEQKEESRGNDDHVTAIREYRSKIETELSGICDGILKLLDSRLIPAAASG
DSKVFYLKMKGDYHRYLAEFKTGQERKDAAEHTLAAYKSAQDIANAELAPTHPIRLGLAL
NFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDR
G

Sequence of entity 2 (K, L, M, N, O, P, Q, R, S, T), FASTA

>8QTT_2 BRI1 kinase inhibitor 1 (chains K, L, M, N, O, P, Q, R, S, T)
ELFSAP

Primary citation

Mechanistic Insights into the Function of 14-3-3 Proteins as Negative Regulators of Brassinosteroid Signaling in Arabidopsis. Obergfell, E., Hohmann, U., Moretti, A. et al. Plant Cell Physiol (2024) 65:1674-1688. DOI 10.1093/pcp/pcae056 · PubMed

Other PDB entries of the same protein (UniProt Q01525 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8QTF 1.9 Å, Crystal structure of a C-terminally truncated version of Arabidopsis thaliana 14-3-3…
8QTC 3.5 Å, Crystal structure of Arabidopsis thaliana 14-3-3 omega in complex with a phosphopeptide…

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