8U8C: TREX-2 complex

Crystal structure of the TREX-2 complex in complex with the N-terminal motif of Sub2. Determined by X-ray diffraction at 2.4 Å resolution. Released 19 Mar 2025.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Saccharomyces cerevisiae S288C
Chains
4
Atoms
7,881
Mol. weight
126.61 kDa
Released
19 Mar 2025

Explore 8U8C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8U8C contains 63 α-helices and 10 β-strands across 4 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: 33 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix91-966
α-helix103-1064
α-helix113-1153
α-helix117-1193
α-helix120-1223
β-strand12811
α-helix138-15316
α-helix157-17721
α-helix206-21510
α-helix220-2223
α-helix238-2414
α-helix248-2514
α-helix252-2543
α-helix258-27114
α-helix273-2753
α-helix280-29617
β-strand29911
α-helix302-32524
α-helix331-35424
α-helix362-37211
α-helix377-3859
α-helix388-3914
α-helix394-40613
α-helix416-4183
α-helix426-4338
α-helix440-4467
α-helix447-4493
α-helix450-46314
α-helix469-4713
β-strand472-47322
α-helix474-4818
α-helix486-49510
β-strand499-50132
β-strand505-50732
α-helix508-5103
α-helix522-5265
α-helix530-5378
α-helix541-5466
Chain B: 27 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix3-1210
α-helix23-3715
α-helix42-509
α-helix59-7416
α-helix80-9617
α-helix106-12924
α-helix131-1344
α-helix140-15415
α-helix158-1603
α-helix170-1734
α-helix175-18814
α-helix192-1943
α-helix195-20511
α-helix211-2133
α-helix216-23217
α-helix236-25116
α-helix258-27720
β-strand28213
α-helix293-30715
α-helix311-32010
α-helix322-3276
α-helix331-35121
α-helix352-3576
β-strand362-36434
α-helix365-37612
α-helix400-40910
β-strand415-41844
β-strand423-42644
α-helix432-4354
α-helix439-4468
α-helix448-4514
Chain C: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix35-373
β-strand6013
α-helix72-8716
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix16-194

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Nuclear mRNA export protein SAC3Aprotein497Saccharomyces cerevisiae S288CP46674 (AlphaFold model)
Nuclear mRNA export protein THP1Bprotein455Saccharomyces cerevisiae S288CQ08231 (AlphaFold model)
26S proteasome complex subunit SEM1Cprotein89Saccharomyces cerevisiae S288CO94742 (AlphaFold model)
ATP-dependent RNA helicase SUB2Dprotein55Saccharomyces cerevisiae S288CQ07478 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8U8C_1 Nuclear mRNA export protein SAC3 (chains A)
GAMGSKSQQPLQNLSHSPSYTENKPDKKKKYMINDAKTIQLVGPLISSPDNLGFQKRSHK
ARELPRFLINQEPQLEKRAFVQDPWDKANQEKMISLEESIDDLNELYETLKKMRNTERSI
MEEKGLVDKADSAKDLYDAIVFQGTCLDMCPTFERSRRNVEYTVYSYEKNQPNDKKASRT
KALKVFARPAAAAAPPLPSDVRPPHILVKTLDYIVDNLLTTLPESEGFLWDRMRSIRQDF
TYQNYSGPEAVDCNERIVRIHLLILHIMVKSNVEFSLQQELEQLHKSLITLSEIYDDVRS
SGGTCPNEAEFRAYALLSKIRDPQYDENIQRLPKHIFQDKLVQMALCFRRVISNSAYTER
GFVKTENCLNFYARFFQLMQSPSLPLLMGFFLQMHLTDIRFYALRALSHTLNKKHKPIPF
IYLENMLLFNNRQEIIEFCNYYSIEIINGDAADLKTLQHYSHKLSETQPLKKTYLTCLER
RLQKTTYKGLINGGEDN
Sequence of entity 2 (B), FASTA
>8U8C_2 Nuclear mRNA export protein THP1 (chains B)
MDMANQLLDELAHGNFSHLTLNLSQNGREIAILQKQLTGFDDKQLETFVEQHPAMPNDTR
FKIMCTSFLNYARDVDPWSAWSSSDLIFEFYQCLINCLINDNAPHIEMLIPVATRETEFI
INLAGKLDSFHLQLHTRSHQFLSHISSILSRLFNSIKPPRGNASSTNIPGKQRILLYLVN
KLNNIYFRIESPQLCSNIFKNFQPKSMLAHFNEYQLDQQIEYRYLLGRYYLLNSQVHNAF
VQFNEAFQSLLNLPLTNQAITRNGTRILNYMIPTGLILGKMVKWGPLRPFLSQETIDNWS
VLYKHVRYGNIQGVSLWLRQNERHLCARQLLIVLLEKLPMVTYRNLIKTVIKSWTTEWGQ
NKLPYSLIERVLQLSIGPTFEDPGAQEITIYNGIHSPKNVENVLVTLINLGLLRANCFPQ
LQLCVVKKTTMIQEIVPPVNERITKMFPAHSHVLW
Sequence of entity 3 (C), FASTA
>8U8C_3 26S proteasome complex subunit SEM1 (chains C)
MSTDVAAAQAQSKIDLTKKKNEEINKKSLEEDDEFEDFPIDTWANGETIKSNAVTQTNIW
EENWDDVEVDDDFTNELKAELDRYKRENQ
Sequence of entity 4 (D), FASTA
>8U8C_4 ATP-dependent RNA helicase SUB2 (chains D)
MSHEGEEDLLEYSDNEQEIQIDASKAAEAGETGAATSATEGDNNNNTAAGDKKGS

Primary citation

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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