5G5P: Saccharomyces cerevisiae TREX-2 complex
Structure of the Saccharomyces cerevisiae TREX-2 complex. Determined by electron microscopy at 5.3 Å resolution. Released 23 Nov 2016.
- Method
- Electron microscopy
- Resolution
- 5.3 Å
- Organism
- SACCHAROMYCES CEREVISIAE
- Chains
- 6
- Atoms
- 6,830
- Mol. weight
- 361.93 kDa
- Released
- 23 Nov 2016
Explore 5G5P in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5G5P contains 55 α-helices and 9 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, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 258-271 | 14 | |
| α-helix | 273-275 | 3 | |
| α-helix | 280-296 | 17 | |
| α-helix | 302-324 | 23 | |
| α-helix | 332-354 | 23 | |
| α-helix | 362-372 | 11 | |
| α-helix | 377-384 | 8 | |
| α-helix | 388-391 | 4 | |
| α-helix | 394-406 | 13 | |
| α-helix | 426-433 | 8 | |
| α-helix | 440-446 | 7 | |
| α-helix | 447-449 | 3 | |
| α-helix | 450-462 | 13 | |
| β-strand | 465 | 1 | 1 |
| α-helix | 469-471 | 3 | |
| β-strand | 472-473 | 2 | 2 |
| α-helix | 474-481 | 8 | |
| α-helix | 486-495 | 10 | |
| β-strand | 500-501 | 2 | 2 |
| β-strand | 505-506 | 2 | 2 |
| α-helix | 508-510 | 3 | |
| α-helix | 522-526 | 5 | |
| α-helix | 530-536 | 7 | |
| α-helix | 541-545 | 5 | |
Chain B: 29 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-12 | 10 | |
| α-helix | 23-37 | 15 | |
| α-helix | 42-50 | 9 | |
| α-helix | 59-74 | 16 | |
| α-helix | 84-96 | 13 | |
| α-helix | 106-128 | 23 | |
| α-helix | 131-134 | 4 | |
| α-helix | 140-155 | 16 | |
| α-helix | 156-160 | 5 | |
| α-helix | 170-173 | 4 | |
| α-helix | 175-188 | 14 | |
| α-helix | 192-194 | 3 | |
| α-helix | 195-200 | 6 | |
| α-helix | 202-205 | 4 | |
| α-helix | 211-213 | 3 | |
| α-helix | 216-232 | 17 | |
| α-helix | 236-252 | 17 | |
| α-helix | 258-277 | 20 | |
| β-strand | 282 | 1 | 3 |
| α-helix | 288-290 | 3 | |
| α-helix | 293-308 | 16 | |
| α-helix | 311-320 | 10 | |
| α-helix | 322-327 | 6 | |
| α-helix | 331-351 | 21 | |
| α-helix | 352-357 | 6 | |
| β-strand | 362-364 | 3 | 1 |
| α-helix | 365-376 | 12 | |
| α-helix | 400-409 | 10 | |
| β-strand | 415-418 | 4 | 1 |
| β-strand | 423-426 | 4 | 1 |
| α-helix | 432-435 | 4 | |
| α-helix | 439-446 | 8 | |
| α-helix | 448-451 | 4 | |
Chain C: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-31 | 4 | |
| α-helix | 35-37 | 3 | |
| β-strand | 60 | 1 | 3 |
| α-helix | 72-87 | 16 | |
Chain D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-16 | 15 | |
Chain E: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-23 | 21 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-10 | 9 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Nuclear mRNA export protein SAC3 | A | protein | 805 | SACCHAROMYCES CEREVISIAE | P46674 (AlphaFold model) |
| Nuclear mRNA export protein THP1 | B | protein | 455 | SACCHAROMYCES CEREVISIAE | Q08231 (AlphaFold model) |
| 26S proteasome complex subunit SEM1 | C | protein | 89 | SACCHAROMYCES CEREVISIAE | O94742 (AlphaFold model) |
| Nuclear mRNA export protein SAC3 | D, E, F | protein | 805 | SACCHAROMYCES CEREVISIAE | |
Sequence of entity 1 (A), FASTA
>5G5P_1 NUCLEAR MRNA EXPORT PROTEIN SAC3 (chains A)
MNTSFGSVVPSTNFNFFKGHGNNDNTSANSTVNNSNFFLNSNETKPSKNVFMVHSTSQKK
SQQPLQNLSHSPSYTENKPDKKKKYMINDAKTIQLVGPLISSPDNLGFQKRSHKARELPR
FLINQEPQLEKRAFVQDPWDKANQEKMISLEESIDDLNELYETLKKMRNTERSIMEEKGL
VDKADSAKDLYDAIVFQGTCLDMCPTFERSRRNVEYTVYSYEKNQPNDKKASRTKALKVF
ARPAAAAAPPLPSDVRPPHILVKTLDYIVDNLLTTLPESEGFLWDRMRSIRQDFTYQNYS
GPEAVDCNERIVRIHLLILHIMVKSNVEFSLQQELEQLHKSLITLSEIYDDVRSSGGTCP
NEAEFRAYALLSKIRDPQYDENIQRLPKHIFQDKLVQMALCFRRVISNSAYTERGFVKTE
NCLNFYARFFQLMQSPSLPLLMGFFLQMHLTDIRFYALRALSHTLNKKHKPIPFIYLENM
LLFNNRQEIIEFCNYYSIEIINGDAADLKTLQHYSHKLSETQPLKKTYLTCLERRLQKTT
YKGLINGGEDNLASSVYVKDPKKDRIPSIADQSFLMENFQNNYNEKLNQNSSVKPQINTS
PKRVATRPNHFPFSQESKQLPQISQSHTLSTNPLLTPQVHGDLSEQKQQQIKTVTDGGSP
FVFDQSAQNSTVEASKAHMISTTSNGAYDEKLSSEQEEMRKKEEQRIEEEKTQLKKKQEN
ADKQVITEQIANDLVKEVVNSSVISIVKREFSEANYRKDFIDTMTRELYDAFLHERLYLI
YMDSRAELKRNSTLKKKFFEKWQAS
Sequence of entity 2 (B), FASTA
>5G5P_2 NUCLEAR MRNA EXPORT PROTEIN THP1 (chains B)
MDMANQLLDELAHGNFSHLTLNLSQNGREIAILQKQLTGFDDKQLETFVEQHPAMPNDTR
FKIMCTSFLNYARDVDPWSAWSSSDLIFEFYQCLINCLINDNAPHIEMLIPVATRETEFI
INLAGKLDSFHLQLHTRSHQFLSHISSILSRLFNSIKPPRGNASSTNIPGKQRILLYLVN
KLNNIYFRIESPQLCSNIFKNFQPKSMLAHFNEYQLDQQIEYRYLLGRYYLLNSQVHNAF
VQFNEAFQSLLNLPLTNQAITRNGTRILNYMIPTGLILGKMVKWGPLRPFLSQETIDNWS
VLYKHVRYGNIQGVSLWLRQNERHLCARQLLIVLLEKLPMVTYRNLIKTVIKSWTTEWGQ
NKLPYSLIERVLQLSIGPTFEDPGAQEITIYNGIHSPKNVENVLVTLINLGLLRANCFPQ
LQLCVVKKTTMIQEIVPPVNERITKMFPAHSHVLW
Sequence of entity 3 (C), FASTA
>5G5P_3 26S PROTEASOME COMPLEX SUBUNIT SEM1 (chains C)
MSTDVAAAQAQSKIDLTKKKNEEINKKSLEEDDEFEDFPIDTWANGETIKSNAVTQTNIW
EENWDDVEVDDDFTNELKAELDRYKRENQ
Sequence of entity 4 (D, E, F), FASTA
>5G5P_4 NUCLEAR MRNA EXPORT PROTEIN SAC3 (chains D, E, F)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
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XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
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Primary citation
The Sac3 Tpr-Like Region in the Saccharomyces Cerevisiae Trex-2 Complex is More Extensive But Independent of the Cid Region. Aibara, S., Bai, X.C., Stewart, M. J Struct Biol (2016) 195:316. DOI 10.1016/J.JSB.2016.07.007 · 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
- 4TRQ 3.1 Å, Crystal structure of Sac3/Thp1/Sem1
- 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
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