5SUQ: THO-Sub2 complex

Crystal structure of the THO-Sub2 complex. Determined by X-ray diffraction at 6.0 Å resolution. Released 18 Jan 2017.

Method: X-ray diffraction
Resolution: 6.0 Å
Organisms: Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Saccharomyces cerevisiae
Chains: 6
Atoms: 30,788
Mol. weight: 592.04 kDa
Ligands: KEG
Released: 18 Jan 2017

Explore 5SUQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5SUQ contains 298 α-helices and 86 β-strands across 6 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.

Chains A and C: 20 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	63-67	5
α-helix	71-79	9
α-helix	87-96	10
β-strand	102-105	4	1
α-helix	113-123	11
β-strand	133-136	4	1
α-helix	140-153	14
β-strand	162-165	4	1
α-helix	171-179	9
β-strand	187-190	4	1
α-helix	192-199	8
β-strand	211-215	5	1
α-helix	217-222	6
α-helix	224-234	11
β-strand	242-247	6	1
α-helix	255-259	5
β-strand	266-268	3	1
β-strand	281-287	7	2
α-helix	290-292	3
α-helix	293-303	11
β-strand	308-312	5	2
α-helix	316-328	13
β-strand	333-336	4	2
β-strand	340	1	3
α-helix	342-353	12
β-strand	359-362	4	2
α-helix	364-366	3
β-strand	375-380	6	2
α-helix	387-394	8
α-helix	399-401	3
β-strand	404-410	7	2
α-helix	413-426	14
β-strand	431-432	2	2
α-helix	433-434	2
α-helix	441-443	3

Chains B and D: 0 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	37-40	4	4
β-strand	50-53	4	5
β-strand	60-63	4	5
β-strand	69-72	4	5
β-strand	79-83	5	5
β-strand	92-95	4	6
β-strand	102-105	4	6
β-strand	110-115	6	6
β-strand	120-126	7	6
β-strand	134-137	4	7
β-strand	144-147	4	7
β-strand	153-156	4	7
β-strand	163-167	5	7
β-strand	176-178	3	8
β-strand	186-189	4	8
β-strand	195-198	4	8
β-strand	207-210	4	8
β-strand	219-221	3	9
β-strand	229-232	4	9
β-strand	238-241	4	9
β-strand	248-252	5	9
β-strand	264-267	4	10
β-strand	273-276	4	10
β-strand	284-286	3	10
β-strand	295-296	2	10
β-strand	306-308	3	4
β-strand	316-319	4	4
β-strand	328-330	3	4

Chain M: 129 helices, 0 β-strands

Element	Residues	Length
α-helix	9-16	8
α-helix	25-37	13
α-helix	45-62	18
α-helix	70-78	9
α-helix	84-97	14
α-helix	109-116	8
α-helix	120-133	14
α-helix	139-149	11
α-helix	159-168	10
α-helix	176-185	10
α-helix	201-220	20
α-helix	233-263	31
α-helix	277-291	15
α-helix	304-318	15
α-helix	333-349	17
α-helix	366-381	16
α-helix	395-410	16
α-helix	426-441	16
α-helix	456-470	15
α-helix	483-491	9
α-helix	2105-2120	16
α-helix	2504-2522	19
α-helix	2538-2557	20
α-helix	2570-2607	38
α-helix	2631-2646	16
α-helix	2664-2680	17
α-helix	2801-2808	8
α-helix	2823-2845	23
α-helix	2858-2894	37
α-helix	2907-2926	20
α-helix	2939-2957	19
α-helix	2972-2991	20
α-helix	3012-3040	29
α-helix	3041-3045	5
α-helix	3046-3051	6
α-helix	3181-3199	19
α-helix	4003-4016	14
α-helix	4064-4075	12
α-helix	4090-4104	15
α-helix	4111-4127	17
α-helix	4137-4144	8
α-helix	4153-4162	10
α-helix	4174-4186	13
α-helix	4200-4216	17
α-helix	4231-4243	13
α-helix	4256-4272	17
α-helix	4287-4302	16
α-helix	4315-4324	10
α-helix	4338-4352	15
α-helix	4367-4379	13
α-helix	4387-4398	12
α-helix	4408-4416	9
α-helix	4432-4442	11
α-helix	4455-4471	17
α-helix	4485-4498	14
α-helix	4512-4524	13
α-helix	4530-4539	10
α-helix	4553-4566	14
α-helix	4579-4587	9
α-helix	4599-4617	19
α-helix	4630-4643	14
α-helix	4672-4687	16
α-helix	4691-4708	18
α-helix	4721-4733	13
α-helix	4747-4762	16
α-helix	4781-4793	13
α-helix	4805-4827	23
α-helix	4842-4853	12
α-helix	4866-4874	9
α-helix	4887-4894	8
α-helix	4906-4930	25
α-helix	4943-4949	7
α-helix	5138-5147	10
α-helix	5198-5210	13
α-helix	5226-5237	12
α-helix	5252-5261	10
α-helix	5274-5288	15
α-helix	6034-6052	19
α-helix	6067-6080	14
α-helix	6093-6111	19
α-helix	6124-6160	37
α-helix	6173-6193	21
α-helix	6211-6241	31
α-helix	6268-6282	15
α-helix	6297-6315	19
α-helix	6328-6349	22
α-helix	6373-6388	16
α-helix	6403-6415	13
α-helix	6432-6441	10
α-helix	6454-6467	14
α-helix	6481-6501	21
α-helix	6515-6531	17
α-helix	6543-6556	14
α-helix	6602-6621	20
α-helix	6637-6646	10
α-helix	6660-6679	20
α-helix	6693-6710	18
α-helix	6725-6743	19
α-helix	6809-6825	17
α-helix	6831-6844	14
α-helix	6857-6870	14
α-helix	6878-6887	10
α-helix	6901-6910	10
α-helix	6925-6934	10
α-helix	7069-7078	10
α-helix	7104-7142	39
α-helix	7148-7166	19
α-helix	7202-7221	20
α-helix	7343-7361	19
α-helix	8093-8105	13
α-helix	8110-8125	16
α-helix	8134-8155	22
α-helix	8167-8178	12
α-helix	8194-8203	10
α-helix	8212-8225	14
α-helix	8235-8252	18
α-helix	8257-8268	12
α-helix	8275-8286	12
α-helix	8290-8298	9
α-helix	8312-8324	13
α-helix	8339-8354	16
α-helix	8368-8378	11
α-helix	8394-8406	13
α-helix	8416-8426	11
α-helix	8433-8441	9
α-helix	8450-8459	10
α-helix	8472-8482	11
α-helix	8486-8497	12
α-helix	8540-8549	10

Chain N: 129 helices, 0 β-strands

Element	Residues	Length
α-helix	10-16	7
α-helix	25-37	13
α-helix	45-62	18
α-helix	70-78	9
α-helix	84-97	14
α-helix	109-116	8
α-helix	120-133	14
α-helix	139-149	11
α-helix	159-168	10
α-helix	176-185	10
α-helix	201-220	20
α-helix	233-263	31
α-helix	277-291	15
α-helix	304-318	15
α-helix	333-349	17
α-helix	366-381	16
α-helix	395-410	16
α-helix	426-441	16
α-helix	456-470	15
α-helix	483-491	9
α-helix	2105-2120	16
α-helix	2504-2522	19
α-helix	2538-2557	20
α-helix	2570-2607	38
α-helix	2631-2646	16
α-helix	2664-2680	17
α-helix	2801-2808	8
α-helix	2823-2845	23
α-helix	2858-2894	37
α-helix	2907-2926	20
α-helix	2939-2957	19
α-helix	2972-2991	20
α-helix	3012-3040	29
α-helix	3041-3045	5
α-helix	3046-3051	6
α-helix	3181-3199	19
α-helix	4003-4016	14
α-helix	4064-4075	12
α-helix	4090-4104	15
α-helix	4111-4127	17
α-helix	4137-4144	8
α-helix	4153-4162	10
α-helix	4174-4186	13
α-helix	4200-4216	17
α-helix	4231-4243	13
α-helix	4256-4272	17
α-helix	4287-4302	16
α-helix	4315-4324	10
α-helix	4338-4352	15
α-helix	4367-4379	13
α-helix	4387-4398	12
α-helix	4408-4416	9
α-helix	4432-4442	11
α-helix	4455-4471	17
α-helix	4485-4498	14
α-helix	4512-4524	13
α-helix	4530-4539	10
α-helix	4553-4566	14
α-helix	4579-4587	9
α-helix	4599-4617	19
α-helix	4630-4643	14
α-helix	4672-4687	16
α-helix	4691-4708	18
α-helix	4721-4733	13
α-helix	4747-4762	16
α-helix	4781-4793	13
α-helix	4805-4827	23
α-helix	4842-4853	12
α-helix	4866-4874	9
α-helix	4887-4894	8
α-helix	4906-4930	25
α-helix	4943-4949	7
α-helix	5138-5147	10
α-helix	5198-5210	13
α-helix	5226-5237	12
α-helix	5252-5261	10
α-helix	5274-5288	15
α-helix	6034-6052	19
α-helix	6067-6080	14
α-helix	6093-6111	19
α-helix	6124-6160	37
α-helix	6173-6193	21
α-helix	6211-6241	31
α-helix	6268-6282	15
α-helix	6297-6315	19
α-helix	6328-6349	22
α-helix	6373-6388	16
α-helix	6403-6415	13
α-helix	6432-6441	10
α-helix	6454-6467	14
α-helix	6481-6501	21
α-helix	6515-6531	17
α-helix	6543-6556	14
α-helix	6602-6621	20
α-helix	6637-6646	10
α-helix	6660-6679	20
α-helix	6693-6710	18
α-helix	6725-6743	19
α-helix	6809-6825	17
α-helix	6831-6844	14
α-helix	6857-6870	14
α-helix	6878-6887	10
α-helix	6901-6910	10
α-helix	6925-6934	10
α-helix	7069-7078	10
α-helix	7104-7142	39
α-helix	7148-7166	19
α-helix	7202-7221	20
α-helix	7343-7361	19
α-helix	8093-8105	13
α-helix	8110-8125	16
α-helix	8134-8155	22
α-helix	8167-8178	12
α-helix	8194-8203	10
α-helix	8212-8225	14
α-helix	8235-8252	18
α-helix	8257-8268	12
α-helix	8275-8286	12
α-helix	8290-8298	9
α-helix	8312-8324	13
α-helix	8339-8354	16
α-helix	8368-8378	11
α-helix	8394-8406	13
α-helix	8416-8426	11
α-helix	8433-8441	9
α-helix	8450-8459	10
α-helix	8472-8482	11
α-helix	8486-8497	12
α-helix	8540-8549	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATP-dependent RNA helicase SUB2	A, C	protein	446	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	Q07478 (AlphaFold model)
Tex1	B, D	protein	400	Saccharomyces cerevisiae
Tho2, Hpr1, Mft1, and Thp2	M, N	protein	2300	Saccharomyces cerevisiae

Sequence of entity 1 (A, C), FASTA

>5SUQ_1 ATP-dependent RNA helicase SUB2 (chains A, C)
MSHEGEEDLLEYSDNEQEIQIDASKAAEAGETGAATSATEGDNNNNTAAGDKKGSYVGIH
STGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLST
LQQLDPVPGEVAVVVICNARELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKN
KDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEELDMRRDVQEIFRATPRD
KQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTLHGLQQYYIKLEEREKNRKLAQL
LDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRIC
VSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEDEEVLA
KIQERFDVKIAEFPEEGIDPSTYLNN

Sequence of entity 2 (B, D), FASTA

>5SUQ_2 Tex1 (chains B, D)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
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XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Sequence of entity 3 (M, N), FASTA

>5SUQ_3 Tho2, Hpr1, Mft1, and Thp2 (chains M, N)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
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Ligands and cofactors

ID	Name	Formula	Copies
KEG	12-tungstophosphate	O40 P W12	11

Primary citation

Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1. Ren, Y., Schmiege, P., Blobel, G. Elife (2017) 6. DOI 10.7554/eLife.20070 · PubMed

Other PDB entries of the same protein (UniProt Q07478 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8U8C 2.4 Å, Crystal structure of the TREX-2 complex in complex with the N-terminal motif of Sub2
5SUP 2.6 Å, Crystal structure of the Sub2-Yra1 complex in association with RNA
8U8D 3.04 Å, Cryo-EM structure of the TREX-2 complex in complex with the N-terminal motif of Sub2
8U8E 3.33 Å, Cryo-EM structure of the TREX-2 complex in association with Sub2
7APX 3.4 Å, yeast THO-Sub2 complex
7V2Y 3.4 Å, cryo-EM structure of yeast THO complex with Sub2
7LUV 3.7 Å, Cryo-EM structure of the yeast THO-Sub2 complex
9ZEB 3.72 Å, Cryo-EM structure of the TREX-2.1 complex (Thp3/Csn12/Sem1) bound to the DEAD-box ATPase…
7AQO 4.5 Å, yeast THO-Sub2 complex dimer

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