3TO9: Yeast Esa1 E338Q HAT domain

Name: PDB 3TO9: Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site lysine acetylated
Published: 2011-11-09
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site lysine acetylated. Determined by X-ray diffraction at 2.0 Å resolution. Released 9 Nov 2011.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 2,610
Mol. weight: 34.44 kDa
Ligands: CAD, COA
Released: 9 Nov 2011

Explore 3TO9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3TO9 contains 9 α-helices and 17 β-strands across 1 chain. 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: 9 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	169-172	4	1
β-strand	175-177	3	1
β-strand	194-197	4	1
β-strand	204-205	2	1
α-helix	208-215	8
β-strand	226-230	5	2
β-strand	234-240	7	2
α-helix	245-256	12
β-strand	271-280	10	2
β-strand	283-293	11	2
β-strand	300-302	3	3
β-strand	305-307	3	2
α-helix	309-311	3
α-helix	316-330	15
β-strand	335	1	4
β-strand	336-337	2	3
α-helix	343-363	21
β-strand	367-369	3	5
α-helix	370-377	8
β-strand	379	1	4
α-helix	381-390	10
β-strand	394-397	4	5
β-strand	400-404	5	5
α-helix	407-418	12
α-helix	426-428	3
β-strand	429	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone acetyltransferase ESA1	A	protein	276	Saccharomyces cerevisiae	Q08649 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3TO9_1 Histone acetyltransferase ESA1 (chains A)
EVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKCT
LRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRR
DELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPQK
PLSDLGLLSYRAYWSDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYYKG
QHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKPPV

Ligands and cofactors

ID	Name	Formula	Copies
CAD	Cacodylic acid	C2 H7 As O2	1
COA	Coenzyme a	C21 H36 N7 O16 P3 S	1

Water and common crystallization additives (SO4, EDO) are not listed.

Primary citation

MYST protein acetyltransferase activity requires active site lysine autoacetylation. Yuan, H., Rossetto, D., Mellert, H. et al. EMBO J (2011) 31:58-70. DOI 10.1038/emboj.2011.382 · PubMed

Other PDB entries of the same protein (UniProt Q08649 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3TO7 1.9 Å, Crystal structure of yeast Esa1 HAT domain bound to coenzyme A with active site lysine…
1FY7 2.0 Å, Crystal structure of yeast ESA1 histone acetyltransferase domain complexed with coenzyme a
3TO6 2.1 Å, Crystal structure of yeast Esa1 HAT domain complexed with H4K16CoA bisubstrate inhibitor
1MJA 2.26 Å, Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl…
1MJ9 2.5 Å, Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A
1MJB 2.5 Å, Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with…
5J9T 2.7 Å, Crystal structure of the NuA4 core complex
5J9W 2.8 Å, Crystal structure of the NuA4 core complex
5J9U 2.95 Å, Crystal structure of the NuA4 core complex
5J9Q 3.25 Å, Crystal structure of the NuA4 core complex
7VVU 3.4 Å, NuA4 HAT module bound to the nucleosome
8X2X 3.8 Å, The piccolo NuA4 bound to the H2A.Z nucleosome complex at pre-H4-acetylation state

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