3Q68: Vacuolar protein sorting-associated protein 75

Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P212121). Determined by X-ray diffraction at 2.71 Å resolution. Released 23 Mar 2011.

Method: X-ray diffraction
Resolution: 2.71 Å
Organism: Saccharomyces cerevisiae
Chains: 3
Atoms: 7,145
Mol. weight: 112.12 kDa
Released: 23 Mar 2011

Explore 3Q68 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3Q68 contains 39 α-helices and 36 β-strands across 3 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: 13 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	9-53	45
α-helix	57-64	8
α-helix	68-71	4
α-helix	74-76	3
α-helix	77-80	4
β-strand	83-90	8	1
α-helix	91-93	3
β-strand	103-109	7	1
β-strand	112	1	2
β-strand	116	1	2
β-strand	119-128	10	1
β-strand	138-141	4	1
α-helix	150-155	6
α-helix	166-175	10
α-helix	179-182	4
α-helix	197-203	7
α-helix	204-208	5
α-helix	212-218	7
α-helix	224-226	3

Chain B: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	4-52	49
α-helix	57-64	8
α-helix	67-69	3
α-helix	74-80	7
β-strand	83-90	8	10
α-helix	91-93	3
β-strand	103-109	7	10
β-strand	112	1	11
β-strand	116	1	11
β-strand	119-128	10	10
β-strand	138-141	4	10
α-helix	151-153	3
α-helix	166-176	11
α-helix	179-183	5
α-helix	197-203	7
α-helix	204-208	5
α-helix	212-222	11

Chain C: 15 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	3-9	7
β-strand	12	1	3
β-strand	16-23	8	4
α-helix	24-26	3
β-strand	27-29	3	4
β-strand	33	1	5
β-strand	43-57	15	4
β-strand	60-74	15	4
β-strand	79-90	12	4
α-helix	100-113	14
β-strand	114	1	6
α-helix	116-120	5
β-strand	123	1	7
β-strand	124	1	4
α-helix	144-158	15
α-helix	164-167	4
α-helix	169-175	7
β-strand	177	1	7
β-strand	186-193	8	4
α-helix	204-206	3
α-helix	215-233	19
β-strand	234	1	8
β-strand	239-243	5	4
α-helix	249-257	9
β-strand	265-266	2	4
β-strand	277	1	9
β-strand	283	1	5
α-helix	289-299	11
β-strand	307	1	9
α-helix	308-317	10
β-strand	328-334	7	4
β-strand	336	1	8
β-strand	342	1	6
β-strand	350	1	4
α-helix	355-366	12
α-helix	373-386	14
α-helix	387-391	5
β-strand	396-399	4	4
β-strand	402	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vacuolar protein sorting-associated protein 75 (VPS75)	A, B	protein	264	Saccharomyces cerevisiae	P53853 (AlphaFold model)
Histone acetyltransferase RTT109	C	protein	442	Saccharomyces cerevisiae	Q07794 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3Q68_1 Vacuolar protein sorting-associated protein 75 (VPS75) (chains A, B)
MMSDQENENEHAKAFLGLAKCEEEVDAIEREVELYRLNKMKPVYEKRDAYIDEIAEFWKI
VLSQHVSFANYIRASDFKYIDTIDKIKVEWLALESEMYDTRDFSITFHFHGIEGDFKEQQ
VTKVFQIKKGKDDQEDGILTSEPVPIEWPQSYDSINPDLIKDKRSPEGKKKYRQGMKTIF
GWFRWTGLKPGKEFPHGDSLASLFSEEIYPFCVKYYAEAQRDLEDEEGESGLSADGDSED
DDGSLGEVDLPLSDEEPSSKKRKV

Sequence of entity 2 (C), FASTA

>3Q68_2 Histone acetyltransferase RTT109 (chains C)
GMDPNSMSLNDFLSSVLPVSEQFEYLSLQSIPLETHAVVTPNKDDKRVPKSTIKTQHFFS
LFHQGKVFFSLEVYVYVTLWDEADAERLIFVSKADTNGYCNTRVSVRDITKIILEFILSI
DPNYYLQKVKPAIRSYKKISPELISAASTPARTLRILARRLKQSGSTVLKEIESPRFQQD
LYLSFTCPREILTKICLFTRPASQYLFPDSSKNSKKHILNGEELMKWWGFILDRLLIECF
QNDTQAKLRIPGEDPARVRSYLRGMKYPLWQVGDIFTSKENSLAVYNIPLFPDDPKARFI
HQLAEEDRLLKVSLSSFWIELQERQEFKLSVTSSVMGISGYSLATPSLFPSSADVIVPKS
RKQFRAIKKYITGEEYDTEEGAIEAFTNIRDFLLLRMATNLQSLTGKREHRERNQPVPAS
NINTLAITMLKPRKKAKALPKT

Primary citation

Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex. Su, D., Hu, Q., Zhou, H. et al. J Biol Chem (2011) 286:15625-15629. DOI 10.1074/jbc.C111.220715 · PubMed

Other PDB entries of the same protein (UniProt P53853 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2ZD7 1.85 Å, The structure of VPS75 (Vacuolar protein sorting-associated protein 75)
3C9D 2.0 Å, Crystal structure of Vps75
3DM7 2.0 Å, Crystal Structure of the Vps75 Histone Chaperone
3C9B 2.42 Å, Crystal structure of SeMet Vps75
3Q66 2.71 Å, Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex…
3Q33 2.8 Å, Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated…
3Q35 3.3 Å, Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated…
5AGC 4.0 Å, Crystallographic forms of the Vps75 tetramer
6O22 Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex…

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