4TRQ: Sac3/Thp1/Sem1

Crystal structure of Sac3/Thp1/Sem1. Determined by X-ray diffraction at 3.1 Å resolution. Released 26 Aug 2015.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Saccharomyces cerevisiae
Chains: 6
Atoms: 10,521
Mol. weight: 151.77 kDa
Released: 26 Aug 2015

Explore 4TRQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4TRQ contains 83 α-helices and 18 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.

Chain A: 20 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	258-272	15
α-helix	273-275	3
α-helix	281-295	15
α-helix	302-324	23
α-helix	334-354	21
α-helix	362-373	12
α-helix	377-385	9
α-helix	388-391	4
α-helix	394-406	13
α-helix	416-418	3
α-helix	426-433	8
α-helix	440-446	7
α-helix	447-449	3
α-helix	450-464	15
α-helix	469-471	3
β-strand	472-473	2	1
α-helix	474-480	7
α-helix	486-495	10
β-strand	500-501	2	1
β-strand	505-506	2	1
α-helix	508-510	3
α-helix	530-537	8
α-helix	541-545	5

Chain B: 21 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	175-188	14
α-helix	192-194	3
α-helix	195-199	5
α-helix	200-202	3
α-helix	205-210	6
α-helix	211-213	3
α-helix	216-232	17
α-helix	236-250	15
α-helix	258-277	20
β-strand	282	1	2
α-helix	284-287	4
α-helix	293-308	16
α-helix	311-320	10
α-helix	322-327	6
α-helix	331-337	7
α-helix	339-351	13
α-helix	352-356	5
β-strand	362-364	3	3
α-helix	365-376	12
β-strand	382	1	4
β-strand	385	1	4
α-helix	397-399	3
α-helix	400-410	11
β-strand	416-418	3	3
β-strand	423-425	3	3
α-helix	432-434	3
α-helix	439-446	8

Chain C: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	35-38	4
β-strand	60	1	2
α-helix	71-86	16

Chain D: 20 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	258-272	15
α-helix	280-296	17
α-helix	302-324	23
α-helix	333-354	22
α-helix	362-372	11
α-helix	377-383	7
α-helix	388-391	4
α-helix	394-406	13
α-helix	416-419	4
α-helix	426-433	8
α-helix	440-446	7
α-helix	447-449	3
α-helix	450-464	15
α-helix	466	1
β-strand	472-473	2	5
α-helix	474-480	7
α-helix	486-496	11
β-strand	500-501	2	5
β-strand	505-506	2	5
α-helix	508-510	3
α-helix	524-526	3
α-helix	530-537	8
α-helix	541-546	6

Chain E: 17 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	175-188	14
α-helix	192-195	4
α-helix	196-200	5
α-helix	205-208	4
α-helix	216-232	17
α-helix	236-251	16
α-helix	260-277	18
β-strand	282	1	6
α-helix	284-287	4
α-helix	293-308	16
α-helix	311-326	16
α-helix	331-351	21
α-helix	352-356	5
β-strand	362-364	3	7
α-helix	365-376	12
α-helix	397-399	3
α-helix	400-409	10
β-strand	415-418	4	7
β-strand	423-426	4	7
α-helix	432-434	3
α-helix	439-446	8

Chain F: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	36-38	3
β-strand	60	1	6
α-helix	68-70	3
α-helix	72-87	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nuclear mRNA export protein SAC3	A, D	protein	299	Saccharomyces cerevisiae	P46674 (AlphaFold model)
Nuclear mRNA export protein THP1	B, E	protein	286	Saccharomyces cerevisiae	Q08231 (AlphaFold model)
26S proteasome complex subunit SEM1	C, F	protein	60	Saccharomyces cerevisiae	O94742 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>4TRQ_1 Nuclear mRNA export protein SAC3 (chains A, D)
SDVRPPHILVKTLDYIVDNLLTTLPESEGFLWDRMRSIRQDFTYQNYSGPEAVDCNERIV
RIHLLILHIMVKSNVEFSLQQELEQLHKSLITLSEIYDDVRSSGGTCPNEAEFRAYALLS
KIRDPQYDENIQRLPKHIFQDKLVQMALCFRRVISNSAYTERGFVKTENCLNFYARFFQL
MQSPSLPLLMGFFLQMHLTDIRFYALRALSHTLNKKHKPIPFIYLENMLLFNNRQEIIEF
CNYYSIEIINGDAADLKTLQHYSHKLSETQPLKKTYLTCLERRLQKTTYKGLINGGEDN

Sequence of entity 2 (B, E), FASTA

>4TRQ_2 Nuclear mRNA export protein THP1 (chains B, E)
GKQRILLYLVNKLNNIYFRIESPQLCSNIFKNFQPKSMLAHFNEYQLDQQIEYRYLLGRY
YLLNSQVHNAFVQFNEAFQSLLNLPLTNQAITRNGTRILNYMIPTGLILGKMVKWGPLRP
FLSQETIDNWSVLYKHVRYGNIQGVSLWLRQNERHLCARQLLIVLLEKLPMVTYRNLIKT
VIKSWTTEWGQNKLPYSLIERVLQLSIGPTFEDPGAQEITIYNGIHSPKNVENVLVTLIN
LGLLRANCFPQLQLCVVKKTTMIQEIVPPVNERITKMFPAHSHVLW

Sequence of entity 3 (C, F), FASTA

>4TRQ_3 26S proteasome complex subunit SEM1 (chains C, F)
EEDDEFEDFPIDTWANGETIKSNAVTQTNIWEENWDDVEVDDDFTNELKAELDRYKRENQ

Primary citation

The Nuclear Pore-Associated TREX-2 Complex Employs Mediator to Regulate Gene Expression. Schneider, M., Hellerschmied, D., Schubert, T. et al. Cell (2015) 162:1016-1028. DOI 10.1016/j.cell.2015.07.059 · PubMed

Other PDB entries of the same protein (UniProt P46674 (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
3FWB 2.5 Å, Sac3:Sus1:Cdc31 complex
4MBE 2.61 Å, Sac3:Sus1:Cdc31:Nup1 complex
3FWC 2.7 Å, Sac3:Sus1:Cdc31 complex
3T5V 2.9 Å, Sac3:Thp1:Sem1 complex
4C31 3.0 Å, Nup1:Sac3:Sus1 complex
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
5L3T 4.93 Å, Structure of the Saccharomyces cerevisiae TREX-2 complex
5G5P 5.3 Å, Structure of the Saccharomyces cerevisiae TREX-2 complex

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