Structure of the SecA-SecY complex with the substrate FtsQ-LacY(+7C) treated with DTT. Determined by electron microscopy at 3.27 Å resolution. Released 26 Feb 2025.
Explore 8YA3 in 3D Show helices and sheets RCSB PDB PDBe
8YA3 contains 19 α-helices and 11 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 | 4-18 | 15 | |
| α-helix | 37-40 | 4 | |
| α-helix | 46-50 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| β-strand | 18-19 | 2 | 3 |
| α-helix | 23-58 | 36 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-10 | 8 | |
| α-helix | 12-32 | 21 | |
| β-strand | 35 | 1 | 1 |
| β-strand | 39 | 1 | 2 |
| β-strand | 68 | 1 | 1 |
| α-helix | 75-87 | 13 | |
| α-helix | 93-99 | 7 | |
| α-helix | 103-133 | 31 | |
| β-strand | 141 | 1 | 2 |
| α-helix | 146-172 | 27 | |
| α-helix | 178-201 | 24 | |
| α-helix | 213-235 | 23 | |
| β-strand | 238-242 | 5 | 3 |
| β-strand | 244 | 1 | 4 |
| β-strand | 261-265 | 5 | 3 |
| α-helix | 272-291 | 20 | |
| α-helix | 295-303 | 9 | |
| α-helix | 311-330 | 20 | |
| α-helix | 333-342 | 10 | |
| β-strand | 346 | 1 | 4 |
| β-strand | 347 | 1 | 5 |
| β-strand | 350 | 1 | 5 |
| α-helix | 354-389 | 36 | |
| α-helix | 400-421 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein translocase subunit SecY | Y | protein | 430 | Geobacillus thermodenitrificans NG80-2 | A4IJK8 (AlphaFold model) |
| Protein translocase subunit SecE | E | protein | 70 | Geobacillus thermodenitrificans NG80-2 | A4IJH4 (AlphaFold model) |
| Cell division protein FtsQ,Lactose permease | B | protein | 78 | Escherichia coli K-12 | P02920 (AlphaFold model), P06136 (AlphaFold model) |
>8YA3_1 Protein translocase subunit SecY (chains Y) MFRTISNFMRVSDIRNKIIFTLLMLIVFRIGTFIPVPSVNTDVLKLQDQLNAFGVLNIFC GGALQNFSIFAMGVMPYITASIIVQLLQMDVVPKFAEWSKQGEMGRRKLAQFTRYFTIVL GFIQALGMSYGFNNLAGGMLIQNPGIGTYLLIAVVLTAGTAFLMWLGEQITAKGVGNGIS IIIFAGIVSGIPTILNQIYAQTFENVGEDLTLNIVRLLLVALAVVAVIVGVIYIQQAFRK IPIQYAKRLEGRNPVGGHSTHLPLKVNPAGVIPVIFAVSFLIAPPTIASFFGTNDVTLWI RRTFDYTHPVGMTIYVVLIIAFTYFYAFVQVNPEQMADNLKKQGGYIPGIRPGKNTQEYV TRILYRLTLVGSLFLAFIAVLPVFFVNFANLPPSAQIGGTSLLIVVGVALETMKQLESQL VKRHYRGFIK
>8YA3_2 Protein translocase subunit SecE (chains E) MQRVTNFFKEVVRELKKVSWPNRKELVNYTAVVLATVAFFTVFFAVIDLGISQLIRLVFE GGHHHHHHHH
>8YA3_3 Cell division protein FtsQ,Lactose permease (chains B) MAKKTILFLLTVLTTVLVSGWVVLGAQYEDGCSGVVILKTLHMFEVPFLLVGAFSISGDG DSPHSYHSGDGDKLPEGV
SecY translocon chaperones protein folding during membrane protein insertion. Ou, X., Ma, C., Sun, D. et al. Cell (2025) 188:1912-1924.e13. DOI 10.1016/j.cell.2025.01.037 · PubMed
Other PDB entries of the same protein (UniProt A4IJK8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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