8I3G: Eaf3-Eaf7 complex

Crystal structure of Eaf3-Eaf7 complex. Determined by X-ray diffraction at 2.4 Å resolution. Released 31 May 2023.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 3,271
Mol. weight: 51.34 kDa
Released: 31 May 2023

Explore 8I3G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8I3G contains 28 α-helices and 6 β-strands across 4 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: 11 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	226-240	15
α-helix	245-247	3
β-strand	253	1	1
α-helix	254-265	12
α-helix	266-268	3
α-helix	272-296	25
α-helix	300-302	3
α-helix	303-315	13
α-helix	322-324	3
β-strand	327	1	1
α-helix	328-343	16
α-helix	349-368	20
α-helix	370-373	4
β-strand	397-398	2	2

Chain B: 12 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	226-236	11
α-helix	237-241	5
β-strand	244-246	3	3
α-helix	254-268	15
α-helix	272-296	25
α-helix	300-302	3
α-helix	303-316	14
α-helix	322-324	3
α-helix	328-343	16
α-helix	349-368	20
α-helix	370-374	5
β-strand	387-389	3	3
α-helix	390-391	2
α-helix	392-399	8

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	113-116	4
α-helix	129-141	13

Chain D: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	111-114	4
α-helix	119-121	3
β-strand	127-128	2	2
α-helix	129-140	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chromatin modification-related protein EAF3	A, B	protein	184	Saccharomyces cerevisiae	Q12432 (AlphaFold model)
Chromatin modification-related protein EAF7	C, D	protein	36	Saccharomyces cerevisiae	P53911 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8I3G_1 Chromatin modification-related protein EAF3 (chains A, B)
PKISLQIPIKLKSVLVDDWEYVTKDKKICRLPADVTVEMVLNKYEHEVSQELESPGSQSQ
LSEYCAGLKLYFDKCLGNMLLYRLERLQYDELLKKSSKDQKPLVPIRIYGAIHLLRLISV
LPELISSTTMDLQSCQLLIKQTEDFLVWLLMHVDEYFNDKDPNRSDDALYVNTSSQYEGV
ALGM

Sequence of entity 2 (C, D), FASTA

>8I3G_2 Chromatin modification-related protein EAF7 (chains C, D)
EETLLELNNRIRVRKQDFTLPWEEYGELILENARKS

Primary citation

Molecular basis for Eaf3-mediated assembly of Rpd3S and NuA4. Chen, Z., Lundy, T., Zhu, Z. et al. Cell Discov (2023) 9:51-51. DOI 10.1038/s41421-023-00565-9 · PubMed

Other PDB entries of the same protein (UniProt Q12432 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8I3F 1.62 Å, Crystal structure of Rco1-Eaf3 with peptide of histone H3 N-terminal
3E9F 1.8 Å, Crystal structure short-form (residue1-113) of Eaf3 chromo domain
3E9G 2.5 Å, Crystal structure long-form (residue1-124) of Eaf3 chromo domain
7YI1 2.8 Å, Cryo-EM structure of Eaf3 CHD bound to H3K36me3 nucleosome
8TOF 2.8 Å, Rpd3S bound to an H3K36Cme3 modified nucleosome
8KD3 2.9 Å, Rpd3S in complex with nucleosome with H3K36MLA modification, H3K9Q mutation and 187bp DNA
8KD5 2.9 Å, Rpd3S in complex with nucleosome with H3K36MLA modification and 187bp DNA, class2
8KD4 2.93 Å, Rpd3S in complex with nucleosome with H3K36MLA modification and 187bp DNA, class1
8HXX 3.0 Å, Cryo-EM structure of the histone deacetylase complex Rpd3S
8KD2 3.02 Å, Rpd3S in complex with 187bp nucleosome
8KD6 3.07 Å, Rpd3S in complex with nucleosome with H3K36MLA modification and 187bp DNA, class3
8KD7 3.09 Å, Rpd3S in complex with nucleosome with H3K36MLA modification and 167bp DNA

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