8QT5: Arabidopsis thaliana 14-3-3 isoform lambda

Crystal structure of Arabidopsis thaliana 14-3-3 isoform lambda in complex with a phosphopeptide from the transcription factor BZR1. Determined by X-ray diffraction at 2.69 Å resolution. Released 25 Oct 2023.

Method: X-ray diffraction
Resolution: 2.69 Å
Organism: Arabidopsis thaliana
Chains: 7
Atoms: 13,654
Mol. weight: 201.81 kDa
Released: 25 Oct 2023

Explore 8QT5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8QT5 contains 89 α-helices and 0 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.

Chain A: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	7-19	13
α-helix	23-37	15
α-helix	45-78	34
α-helix	82-109	28
α-helix	110-114	5
α-helix	115-117	3
α-helix	121-141	21
α-helix	146-168	23
α-helix	174-185	12
α-helix	186-190	5
α-helix	194-210	17
α-helix	220-239	20

Chain B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	7-19	13
α-helix	23-37	15
α-helix	45-79	35
α-helix	83-109	27
α-helix	110-114	5
α-helix	115-117	3
α-helix	121-141	21
α-helix	144-168	25
α-helix	174-185	12
α-helix	186-190	5
α-helix	194-212	19
α-helix	220-240	21

Chain C: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	7-20	14
α-helix	23-37	15
α-helix	45-77	33
α-helix	82-109	28
α-helix	110-114	5
α-helix	115-117	3
α-helix	121-141	21
α-helix	145-168	24
α-helix	174-185	12
α-helix	186-190	5
α-helix	194-210	17
α-helix	217-241	25
α-helix	1170-1172	3

Chain D: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	7-20	14
α-helix	23-37	15
α-helix	42-44	3
α-helix	45-79	35
α-helix	82-109	28
α-helix	110-114	5
α-helix	115-117	3
α-helix	121-141	21
α-helix	145-168	24
α-helix	174-185	12
α-helix	186-190	5
α-helix	194-210	17
α-helix	217-243	27

Chain E: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	7-19	13
α-helix	23-37	15
α-helix	45-79	35
α-helix	82-109	28
α-helix	110-114	5
α-helix	115-117	3
α-helix	121-141	21
α-helix	144-168	25
α-helix	174-185	12
α-helix	186-190	5
α-helix	194-210	17
α-helix	212-214	3
α-helix	220-242	23

Chain F: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	7-20	14
α-helix	23-37	15
α-helix	42-44	3
α-helix	45-77	33
α-helix	82-109	28
α-helix	110-114	5
α-helix	115-117	3
α-helix	121-141	21
α-helix	144-168	25
α-helix	174-185	12
α-helix	186-190	5
α-helix	194-210	17
α-helix	217-237	21

Chain G: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	7-19	13
α-helix	23-37	15
α-helix	42-44	3
α-helix	45-79	35
α-helix	82-109	28
α-helix	110-114	5
α-helix	115-117	3
α-helix	121-141	21
α-helix	145-168	24
α-helix	174-185	12
α-helix	186-190	5
α-helix	194-210	17
α-helix	220-238	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3-like protein G-BOX factor 14 lambda,Protein BRASSINAZOLE-RESISTANT 1	A, B, C, D, E, F, G	protein	255	Arabidopsis thaliana	P48349 (AlphaFold model), Q8S307 (AlphaFold model)

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

>8QT5_1 14-3-3-like protein G-BOX factor 14 lambda,Protein BRASSINAZOLE-RESISTANT 1 (chains A, B, C, D, E, F, G)
MAATLGRDQYVYMAKLAEQAERYEEMVQFMEQLVTGATPAEELTVEERNLLSVAYKNVIG
SLRAAWRIVSSIEQKEESRKNDEHVSLVKDYRSKVESELSSVCSGILKLLDSHLIPSAGA
SESKVFYLKMKGDYHRYMAEFKSGDERKTAAEDTMLAYKAAQDIAAADMAPTHPIRLGLA
LNFSVFYYEILNSSDKACNMAKQAFEEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSD
MQEQMDEARISNSAP

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

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