8UAH: BACH1 BTB domain-bound FBXL17 ubiquitin ligase

Name: PDB 8UAH: Structure of BACH1 BTB domain-bound FBXL17 ubiquitin ligase
Published: 2024-11-06
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Structure of BACH1 BTB domain-bound FBXL17 ubiquitin ligase. Determined by electron microscopy at 3.3 Å resolution. Released 6 Nov 2024.

Method: Electron microscopy
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,534
Mol. weight: 58.85 kDa
Released: 6 Nov 2024

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

Secondary structure: helices and β-sheets

8UAH contains 20 α-helices and 23 β-strands across 2 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 B: 13 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	380-383	4
β-strand	390	1	1
α-helix	401-403	3
β-strand	416-419	4	1
α-helix	427-433	7
β-strand	442-445	4	1
α-helix	453-456	4
β-strand	468-471	4	1
α-helix	479-487	9
β-strand	494	1	1
β-strand	497	1	2
α-helix	505-508	4
β-strand	520-522	3	1
β-strand	523	1	2
α-helix	530-533	4
β-strand	544-546	3	1
β-strand	548	1	3
α-helix	556-562	7
β-strand	570-571	2	1
β-strand	574	1	3
α-helix	581-590	10
β-strand	596-597	2	1
β-strand	600	1	4
α-helix	608-614	7
β-strand	621-622	2	1
β-strand	625	1	4
α-helix	634-641	8
β-strand	647-649	3	1
α-helix	660-663	4
β-strand	672-674	3	1
α-helix	682-687	6

Chain C: 7 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	21-29	9
β-strand	36-40	5	5
β-strand	43-47	5	5
α-helix	50-55	6
α-helix	57-64	8
β-strand	71-74	4	5
α-helix	81-84	4
α-helix	88-93	6
β-strand	99	1	6
β-strand	102	1	6
α-helix	104-113	10
α-helix	125-131	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
F-box/LRR-repeat protein 17	B	protein	392	Homo sapiens	Q9UF56 (AlphaFold model)
Transcription regulator protein BACH1	C	protein	126	Homo sapiens	O14867 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>8UAH_1 F-box/LRR-repeat protein 17 (chains B)
CHREPPPETPDINQLPPSILLKIFSNLSLDERCLSASLVCKYWRDLCLDFQFWKQLDLSS
RQQVTDELLEKIASRSQNIIEINISDCRSMSDNGVCVLAFKCPGLLRYTAYRCKQLSDTS
IIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMIVIAKGC
LKLQRIYMQENKLVTDQSVKAFAEHCPELQYVGFMGCSVTSKGVIHLTKLRNLSSLDLRH
ITELDNETVMEIVKRCKNLSSLNLCLNWIINDRCVEVIAKEGQNLKELYLVSCKITDYAL
IAIGRYSMTIETVDVGWCKEITDQGATLIAQSSKSLRYLGLMRCDKVNEVTVEQLVQQYP
HITFSTVLQDCKRTLERAYQMGWTPNMSAASS

Sequence of entity 2 (C), FASTA

>8UAH_2 Transcription regulator protein BACH1 (chains C)
SVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIVGQ
ADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQFL
KFKFLD

Primary citation

Recognition of BACH1 quaternary structure degrons by two F-box proteins under oxidative stress. Cao, S., Garcia, S.F., Shi, H. et al. Cell (2024) 187:7568-7584.e22. DOI 10.1016/j.cell.2024.10.012 · PubMed

Other PDB entries of the same protein (UniProt Q9UF56 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8UBT 3.1 Å, Structure of SCF-FBXL17-BACH1BTB E3 ligase complex
6W66 3.21 Å, The structure of the F64A, S172A mutant Keap1-BTB domain in complex with SKP1-FBXL17
8UBV 4.1 Å, Cryo-EM structure of dimeric FBXL17-BACH1BTB E3 ubiquitin ligase complex
8UBU 4.6 Å, Cryo-EM structure of dimeric SCF-FBXL17-BACH1BTB E3 ligase complex close conformation
6WCQ 8.5 Å, Structure of a substrate-bound DQC ubiquitin ligase

Browse structure collections

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