8U77: Taf14

Crystal structure of Taf14 in complex with Yng1. Determined by X-ray diffraction at 1.93 Å resolution. Released 21 Aug 2024.

Method: X-ray diffraction
Resolution: 1.93 Å
Organism: Saccharomyces cerevisiae
Chains: 8
Atoms: 2,881
Mol. weight: 37.98 kDa
Released: 21 Aug 2024

Explore 8U77 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8U77 contains 20 α-helices and 14 β-strands across 8 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: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	179-186	8
α-helix	191-204	14
α-helix	207-209	3
β-strand	212-214	3	1
β-strand	219-223	5	1
α-helix	224-226	3
α-helix	229-241	13

Chain B: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	1393-1400	8	1
α-helix	1401-1402	2

Chain C: 4 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	173-174	2	2
β-strand	177-178	2	2
α-helix	179-186	8
α-helix	191-204	14
β-strand	212-214	3	1
β-strand	219-222	4	1
α-helix	224-226	3
α-helix	229-241	13

Chains D, F and H: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	1393-1400	8	1

Chain E: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	179-186	8
α-helix	191-204	14
α-helix	207-209	3
β-strand	212-214	3	3
β-strand	219-222	4	3
α-helix	224-226	3
α-helix	229-241	13

Chain G: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	179-186	8
α-helix	191-204	14
α-helix	207-209	3
β-strand	212-214	3	3
β-strand	219-222	4	3
α-helix	224-226	3
α-helix	229-242	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcription initiation factor TFIID subunit 14	A, C, E, G	protein	72	Saccharomyces cerevisiae	P35189 (AlphaFold model)
Protein YNG1	B, D, F, H	protein	12	Saccharomyces cerevisiae	Q08465 (AlphaFold model)

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

>8U77_1 Transcription initiation factor TFIID subunit 14 (chains A, C, E, G)
SVKGSVDLEKLAFGLTKLNEDDLVGVVQMVTDNKTPEMNVTNNVEEGEFIIDLYSLPEGL
LKSLWDYVKKNT

Sequence of entity 2 (B, D, F, H), FASTA

>8U77_2 Protein YNG1 (chains B, D, F, H)
EPKLLLKINLKK

Primary citation

Molecular insight into interactions between the Taf14, Yng1 and Sas3 subunits of the NuA3 complex. Nguyen, M.C., Rostamian, H., Raman, A. et al. Nat Commun (2024) 15:5335-5335. DOI 10.1038/s41467-024-49730-y · PubMed

Other PDB entries of the same protein (UniProt P35189 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7UHE 1.66 Å, Taf14 ET domain in complex with C-terminal tail of Taf2
3QRL 1.7 Å, Crystal Structure of the Taf14 YEATS domain
6MIQ 1.75 Å, Crystal structure of Taf14 YEATS domain in complex with histone H3K9bu
6MIO 1.85 Å, Crystal structure of Taf14 YEATS domain in complex with histone H3K9pr
5D7E 1.9 Å, Crystal structure of Taf14 YEATS domain in complex with H3K9ac
6MIN 1.9 Å, Crystal structure of Taf14 YEATS domain G82A mutant in complex with histone H3K9cr
6MIP 2.0 Å, Crystal structure of Taf14 YEATS domain G82A mutant
7F4A 2.0 Å, Crystal structure of Taf14 YEATS domain in complex with H3K9bz peptide
5IOK 2.22 Å, Crystal structure of Taf14 YEATS domain in complex with histone H3K9cr
9VKW 3.13 Å, Cryo-EM structure of the NuA3 complex bound to Ace-coenzyme A
9UUS 3.2 Å, The NuA3 histone acetyltransferase complex bound to acetyl-CoA and H3 tail
9UUO 3.68 Å, The NuA3 histone acetyltransferase complex

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