3Q33: Histone acetyltransferase RTT109

Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation. Determined by X-ray diffraction at 2.8 Å resolution. Released 2 Feb 2011.

Method: X-ray diffraction
Resolution: 2.8 Å
Organisms: Saccharomyces cerevisiae, synthetic
Chains: 3
Atoms: 5,077
Mol. weight: 80.01 kDa
Ligands: ACO
Released: 2 Feb 2011

Explore 3Q33 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3Q33 contains 28 α-helices and 24 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 A: 15 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	3-8	6
β-strand	12	1	1
β-strand	16-23	8	2
α-helix	24-26	3
β-strand	27-29	3	2
β-strand	33	1	3
α-helix	34-36	3
β-strand	45-57	13	2
β-strand	60-73	14	2
β-strand	79-90	12	2
α-helix	100-113	14
α-helix	116-120	5
β-strand	123	1	4
β-strand	124	1	2
α-helix	144-153	10
β-strand	177	1	4
β-strand	186-193	8	2
α-helix	204-206	3
α-helix	215-233	19
β-strand	234	1	5
β-strand	239-243	5	2
α-helix	249-256	8
β-strand	264-266	3	2
α-helix	278-280	3
β-strand	283	1	3
α-helix	289-299	11
α-helix	308-316	9
β-strand	328-334	7	2
β-strand	336	1	5
β-strand	350	1	2
α-helix	355-366	12
α-helix	373-391	19
α-helix	395	1
β-strand	396-399	4	2
β-strand	402	1	1

Chain B: 13 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-53	44
α-helix	57-64	8
α-helix	67-71	5
α-helix	74-76	3
α-helix	77-80	4
β-strand	83-90	8	6
α-helix	91-93	3
β-strand	103-112	10	6
β-strand	116-128	13	6
β-strand	138-141	4	6
α-helix	151-153	3
α-helix	157-159	3
α-helix	166-175	10
α-helix	181-183	3
α-helix	197-203	7
α-helix	204-208	5
α-helix	209-219	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone acetyltransferase RTT109	A	protein	438	Saccharomyces cerevisiae	Q07794 (AlphaFold model)
Vacuolar protein sorting-associated protein 75	B	protein	232	Saccharomyces cerevisiae	P53853 (AlphaFold model)
Histone H3	D	protein	15	synthetic	P61830 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3Q33_1 Histone acetyltransferase RTT109 (chains A)
GSMSLNDFLSSVLPVSEQFEYLSLQSIPLETHAVVTPNKDDKRVPKSTIKTQHFFSLFHQ
GKVFFSLEVYVYVTLWDEADAERLIFVSKADTNGYCNTRVSVRDITKIILEFILSIDPNY
YLQKVKPAIRSYKKISPELISAASTPARTLRILARRLKQSGSTVLKEIESPRFQQDLYLS
FTCPREILTKICLFTRPASQYLFPDSSKNSKKHILNGEELMKWWGFILDRLLIECFQNDT
QAKLRIPGEDPARVRSYLRGMKYPLWQVGDIFTSKENSLAVYNIPLFPDDPKARFIHQLA
EEDRLLKVSLSSFWIELQERQEFKLSVTSSVMGISGYSLATPSLFPSSADVIVPKSRKQF
RAIKKYITGEEYDTEEGAIEAFTNIRDFLLLRMATNLQSLTGKREHRERNQPVPASNINT
LAITMLKPRKKAKALPKT

Sequence of entity 2 (B), FASTA

>3Q33_2 Vacuolar protein sorting-associated protein 75 (chains B)
MMSDQENENEHAKAFLGLAKCEEEVDAIEREVELYRLNKMKPVYEKRDAYIDEIAEFWKI
VLSQHVSFANYIRASDFKYIDTIDKIKVEWLALESEMYDTRDFSITFHFHGIEGDFKEQQ
VTKVFQIKKGKDDQEDGILTSEPVPIEWPQSYDSINPDLIKDKRSPEGKKKYRQGMKTIF
GWFRWTGLKPGKEFPHGDSLASLFSEEIYPFCVKYYAEAQRDLEDEEGESGL

Sequence of entity 3 (D), FASTA

>3Q33_3 HISTONE H3 (chains D)
ARTKQTARKSTGGKX

Ligands and cofactors

ID	Name	Formula	Copies
ACO	Acetyl coenzyme *a	C23 H38 N7 O17 P3 S	1

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

Primary citation

Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation. Tang, Y., Holbert, M.A., Delgoshaie, N. et al. Structure (2011) 19:221-231. DOI 10.1016/j.str.2010.12.012 · PubMed

Other PDB entries of the same protein (UniProt Q07794 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2ZFN 1.9 Å, Self-acetylation mediated histone H3 lysine 56 acetylation by rtt109
3CZ7 2.0 Å, Molecular Basis for the Autoregulation of the Protein Acetyl Transferase Rtt109
2RIM 2.2 Å, Crystal structure of Rtt109
3Q66 2.71 Å, Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex…
3Q68 2.71 Å, Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex…
3QM0 3.1 Å, Crystal structure of RTT109-AC-CoA complex
3Q35 3.3 Å, Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated…
6F0Y Rtt109 peptide bound to Asf1
6O22 Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex…

Browse structure collections

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