Cryo-EM structure of the TREX-2 complex in complex with the N-terminal motif of Sub2. Determined by electron microscopy at 3.04 Å resolution. Released 5 Feb 2025.
Explore 8U8D in 3D Show helices and sheets RCSB PDB PDBe
8U8D contains 52 α-helices and 12 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 90-96 | 7 | |
| α-helix | 116-119 | 4 | |
| α-helix | 120-122 | 3 | |
| α-helix | 126-127 | 2 | |
| β-strand | 128 | 1 | 1 |
| α-helix | 138-153 | 16 | |
| α-helix | 157-178 | 22 | |
| α-helix | 206-215 | 10 | |
| β-strand | 223 | 1 | 2 |
| β-strand | 231 | 1 | 2 |
| α-helix | 249-251 | 3 | |
| α-helix | 258-272 | 15 | |
| α-helix | 273-275 | 3 | |
| α-helix | 280-297 | 18 | |
| β-strand | 299 | 1 | 1 |
| α-helix | 302-325 | 24 | |
| α-helix | 331-354 | 24 | |
| α-helix | 362-372 | 11 | |
| α-helix | 378-384 | 7 | |
| 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 | |
| α-helix | 469-471 | 3 | |
| β-strand | 472-473 | 2 | 3 |
| α-helix | 474-481 | 8 | |
| α-helix | 486-495 | 10 | |
| β-strand | 499-501 | 3 | 3 |
| β-strand | 505-507 | 3 | 3 |
| α-helix | 508-510 | 3 | |
| α-helix | 522-526 | 5 | |
| α-helix | 530-537 | 8 | |
| α-helix | 541-546 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-12 | 9 | |
| α-helix | 27-37 | 11 | |
| α-helix | 42-50 | 9 | |
| α-helix | 59-73 | 15 | |
| α-helix | 84-99 | 16 | |
| α-helix | 106-129 | 24 | |
| α-helix | 140-155 | 16 | |
| α-helix | 170-173 | 4 | |
| α-helix | 175-188 | 14 | |
| α-helix | 192-194 | 3 | |
| α-helix | 195-205 | 11 | |
| α-helix | 211-213 | 3 | |
| α-helix | 216-232 | 17 | |
| α-helix | 236-252 | 17 | |
| α-helix | 259-277 | 19 | |
| β-strand | 282 | 1 | 4 |
| α-helix | 293-307 | 15 | |
| α-helix | 311-320 | 10 | |
| α-helix | 322-327 | 6 | |
| α-helix | 331-354 | 24 | |
| β-strand | 362-364 | 3 | 5 |
| α-helix | 365-376 | 12 | |
| α-helix | 400-410 | 11 | |
| β-strand | 415-418 | 4 | 5 |
| β-strand | 423-426 | 4 | 5 |
| α-helix | 432-434 | 3 | |
| α-helix | 439-446 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 60 | 1 | 4 |
| α-helix | 72-87 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear mRNA export factor | A | protein | 497 | Saccharomyces cerevisiae | P46674 (AlphaFold model) |
| THP1 isoform 1 | B | protein | 455 | Saccharomyces cerevisiae | Q08231 (AlphaFold model) |
| 26S proteasome complex subunit SEM1 | C | protein | 89 | Saccharomyces cerevisiae | O94742 (AlphaFold model) |
| RNA helicase | D | protein | 446 | Saccharomyces cerevisiae | Q07478 (AlphaFold model) |
>8U8D_1 Nuclear mRNA export factor (chains A) GAMGSKSQQPLQNLSHSPSYTENKPDKKKKYMINDAKTIQLVGPLISSPDNLGFQKRSHK ARELPRFLINQEPQLEKRAFVQDPWDKANQEKMISLEESIDDLNELYETLKKMRNTERSI MEEKGLVDKADSAKDLYDAIVFQGTCLDMCPTFERSRRNVEYTVYSYEKNQPNDKKASRT KALKVFARPAAAAAPPLPSDVRPPHILVKTLDYIVDNLLTTLPESEGFLWDRMRSIRQDF TYQNYSGPEAVDCNERIVRIHLLILHIMVKSNVEFSLQQELEQLHKSLITLSEIYDDVRS SGGTCPNEAEFRAYALLSKIRDPQYDENIQRLPKHIFQDKLVQMALCFRRVISNSAYTER GFVKTENCLNFYARFFQLMQSPSLPLLMGFFLQMHLTDIRFYALRALSHTLNKKHKPIPF IYLENMLLFNNRQEIIEFCNYYSIEIINGDAADLKTLQHYSHKLSETQPLKKTYLTCLER RLQKTTYKGLINGGEDN
>8U8D_2 THP1 isoform 1 (chains B) MDMANQLLDELAHGNFSHLTLNLSQNGREIAILQKQLTGFDDKQLETFVEQHPAMPNDTR FKIMCTSFLNYARDVDPWSAWSSSDLIFEFYQCLINCLINDNAPHIEMLIPVATRETEFI INLAGKLDSFHLQLHTRSHQFLSHISSILSRLFNSIKPPRGNASSTNIPGKQRILLYLVN KLNNIYFRIESPQLCSNIFKNFQPKSMLAHFNEYQLDQQIEYRYLLGRYYLLNSQVHNAF VQFNEAFQSLLNLPLTNQAITRNGTRILNYMIPTGLILGKMVKWGPLRPFLSQETIDNWS VLYKHVRYGNIQGVSLWLRQNERHLCARQLLIVLLEKLPMVTYRNLIKTVIKSWTTEWGQ NKLPYSLIERVLQLSIGPTFEDPGAQEITIYNGIHSPKNVENVLVTLINLGLLRANCFPQ LQLCVVKKTTMIQEIVPPVNERITKMFPAHSHVLW
>8U8D_3 26S proteasome complex subunit SEM1 (chains C) MSTDVAAAQAQSKIDLTKKKNEEINKKSLEEDDEFEDFPIDTWANGETIKSNAVTQTNIW EENWDDVEVDDDFTNELKAELDRYKRENQ
>8U8D_4 RNA helicase (chains D) MSHEGEEDLLEYSDNEQEIQIDASKAAEAGETGAATSATEGDNNNNTAAGDKKGSYVGIH STGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLST LQQLFPVPGEVAVVVICNARELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKN KDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEELDMRRDVQEIFRATPRD KQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTLHGLQQYYIKLEEREKNRKLAQL LDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRIC VSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEDEEVLA KIQERFDVKIAEFPEEGIDPSTYLNN
Structures and mRNP remodeling mechanism of the TREX-2 complex. Xie, Y., Clarke, B.P., Xie, D. et al. Structure (2025) 33:566-582.e6. DOI 10.1016/j.str.2024.12.019 · PubMed
Other PDB entries of the same protein (UniProt P46674 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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