8YA0: Protein translocase subunit SecA
Structure of the SecA-SecY complex with the substrate FtsQ-LacY(+7C). Determined by electron microscopy at 2.97 Å resolution. Released 26 Feb 2025.
- Method
- Electron microscopy
- Resolution
- 2.97 Å
- Organisms
- Bacillus subtilis subsp. subtilis str. 168, Geobacillus thermodenitrificans NG80-2, Lama glama
- Chains
- 7
- Atoms
- 13,920
- Mol. weight
- 200.4 kDa
- Ligands
- BEF, MG, ADP
- Released
- 26 Feb 2025
Explore 8YA0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8YA0 contains 69 α-helices and 69 β-strands across 7 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: 42 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-32 | 18 | |
| α-helix | 43-54 | 12 | |
| α-helix | 62-76 | 15 | |
| α-helix | 83-93 | 11 | |
| β-strand | 97-99 | 3 | 1 |
| α-helix | 100-101 | 2 | |
| α-helix | 106-117 | 12 | |
| β-strand | 124-128 | 5 | 1 |
| α-helix | 131-148 | 18 | |
| β-strand | 152-154 | 3 | 1 |
| α-helix | 161-168 | 8 | |
| β-strand | 172-176 | 5 | 1 |
| α-helix | 177-187 | 11 | |
| α-helix | 193-195 | 3 | |
| β-strand | 203-207 | 5 | 1 |
| α-helix | 209 | 1 | |
| α-helix | 210-215 | 6 | |
| α-helix | 216-218 | 3 | |
| β-strand | 220-226 | 7 | 2 |
| α-helix | 232-241 | 10 | |
| α-helix | 245-249 | 5 | |
| β-strand | 250-253 | 4 | 3 |
| β-strand | 258-261 | 4 | 3 |
| α-helix | 263-272 | 10 | |
| α-helix | 284-294 | 11 | |
| α-helix | 295-299 | 5 | |
| α-helix | 302-305 | 4 | |
| β-strand | 306-309 | 4 | 4 |
| β-strand | 312-316 | 5 | 4 |
| α-helix | 317 | 1 | |
| β-strand | 323-324 | 2 | 4 |
| β-strand | 327-329 | 3 | 2 |
| α-helix | 333-341 | 9 | |
| β-strand | 349-356 | 8 | 2 |
| α-helix | 357-361 | 5 | |
| β-strand | 367-371 | 5 | 1 |
| α-helix | 375-377 | 3 | |
| α-helix | 378-383 | 6 | |
| β-strand | 389-391 | 3 | 1 |
| β-strand | 400-402 | 3 | 5 |
| α-helix | 403-405 | 3 | |
| β-strand | 406-408 | 3 | 6 |
| α-helix | 411-426 | 16 | |
| β-strand | 432-435 | 4 | 5 |
| α-helix | 439-450 | 12 | |
| β-strand | 456-459 | 4 | 5 |
| α-helix | 464-466 | 3 | |
| α-helix | 467-473 | 7 | |
| β-strand | 480-483 | 4 | 5 |
| α-helix | 493-495 | 3 | |
| α-helix | 499-501 | 3 | |
| β-strand | 506-509 | 4 | 5 |
| α-helix | 516-527 | 12 | |
| β-strand | 533-537 | 5 | 5 |
| β-strand | 538-540 | 3 | 6 |
| α-helix | 544-549 | 6 | |
| α-helix | 554-556 | 3 | |
| α-helix | 573-618 | 46 | |
| α-helix | 624-641 | 18 | |
| α-helix | 654-664 | 11 | |
| α-helix | 673-675 | 3 | |
| α-helix | 681-703 | 23 | |
| α-helix | 706-741 | 36 | |
| α-helix | 742-744 | 3 | |
| α-helix | 748-776 | 29 | |
Chain B: 4 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-19 | 17 | |
| α-helix | 20-23 | 4 | |
| α-helix | 37-42 | 6 | |
| α-helix | 46-50 | 5 | |
| β-strand | 64-67 | 4 | 2 |
Chain C: 2 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-7 | 3 | 15 |
| β-strand | 21-23 | 3 | 15 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 16 |
| β-strand | 46-51 | 6 | 16 |
| β-strand | 57-59 | 3 | 16 |
| β-strand | 70-72 | 3 | 15 |
| β-strand | 77-79 | 3 | 15 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 16 |
| β-strand | 102-103 | 2 | 16 |
| β-strand | 107-109 | 3 | 16 |
Chain E: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-15 | 13 | |
| β-strand | 18-19 | 2 | 9 |
| α-helix | 23-58 | 36 | |
Chain G: 1 helix, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-22 | 11 | 17 |
| β-strand | 25-36 | 12 | 17 |
| β-strand | 41-48 | 8 | 17 |
| α-helix | 58-61 | 4 | |
| β-strand | 92-100 | 9 | 17 |
| β-strand | 105-115 | 11 | 17 |
| β-strand | 118-128 | 11 | 17 |
| β-strand | 141 | 1 | 18 |
| β-strand | 148-155 | 8 | 17 |
| β-strand | 160-170 | 11 | 17 |
| β-strand | 171 | 1 | 18 |
| β-strand | 176-187 | 12 | 17 |
| β-strand | 199-208 | 10 | 17 |
| β-strand | 217-227 | 11 | 17 |
Chain V: 1 helix, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 11 |
| β-strand | 12 | 1 | 12 |
| β-strand | 17-24 | 8 | 11 |
| β-strand | 33-37 | 5 | 13 |
| β-strand | 47-52 | 6 | 13 |
| β-strand | 58 | 1 | 13 |
| β-strand | 67-72 | 6 | 11 |
| β-strand | 77-83 | 7 | 11 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-93 | 3 | 14 |
| β-strand | 94-98 | 5 | 13 |
| β-strand | 106 | 1 | 13 |
| β-strand | 111-113 | 3 | 14 |
| β-strand | 115 | 1 | 12 |
Chain Y: 17 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-8 | 6 | |
| α-helix | 12-32 | 21 | |
| β-strand | 35 | 1 | 7 |
| α-helix | 36 | 1 | |
| α-helix | 41-46 | 6 | |
| β-strand | 57-60 | 4 | 8 |
| β-strand | 63-66 | 4 | 8 |
| β-strand | 68 | 1 | 7 |
| α-helix | 75-88 | 14 | |
| α-helix | 93-101 | 9 | |
| α-helix | 105-136 | 32 | |
| α-helix | 146-172 | 27 | |
| α-helix | 178-201 | 24 | |
| α-helix | 213-235 | 23 | |
| β-strand | 238-242 | 5 | 9 |
| β-strand | 244-245 | 2 | 10 |
| β-strand | 261-265 | 5 | 9 |
| α-helix | 272-289 | 18 | |
| α-helix | 295-303 | 9 | |
| α-helix | 309-330 | 22 | |
| α-helix | 333-343 | 11 | |
| β-strand | 345-346 | 2 | 10 |
| α-helix | 354-387 | 34 | |
| α-helix | 400-420 | 21 | |
| α-helix | 421-423 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein translocase subunit SecA | A | protein | 765 | Bacillus subtilis subsp. subtilis str. 168 | P28366 (AlphaFold model) |
| Protein translocase subunit SecY | Y | protein | 429 | Geobacillus thermodenitrificans NG80-2 | A4IJK8 (AlphaFold model) |
| Protein translocase subunit SecE | E | protein | 58 | Geobacillus thermodenitrificans NG80-2 | A4IJH4 (AlphaFold model) |
| Nanobody | V | protein | 116 | Lama glama | |
| Cell division protein FtsQ,Lactose permease | B | protein | 72 | Escherichia coli K-12 | P02920 (AlphaFold model), Q7CR81 |
| Nanobody | C | protein | 113 | Lama glama | |
| Green fluorescent protein | G | protein | 225 | Aequorea victoria | P42212 |
Sequence of entity 1 (A), FASTA
>8YA0_1 Protein translocase subunit SecA (chains A)
RTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDDLLVEAFAVVREAS
RRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALTGKGVHVVTVNEYL
ASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNELGFDYLRDNMVLYK
EQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAFVRTLKAEKDYTYD
IKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAMQKDVDYVVEDGQV
VIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNYFRMYEKLAGMTGT
AKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAEDVAQRYMTGQPVL
VGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAVTIATNMAGRGTDI
KLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLSMEDELMRRFGAER
TMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYDDVLRQQREVIYKQ
RFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDLINTTYLDEGALEK
SDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAVDSKWMDHIDAMDQ
LRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKA
Sequence of entity 2 (Y), FASTA
>8YA0_2 Protein translocase subunit SecY (chains Y)
FRTISNFMRVSDIRNKIIFTLLMLIVFRIGTFIPVPSVNTDVLKLQDQLNAFGVLNIFCG
GALQNFSIFAMGVMPYITASIIVQLLQMDVVPKFAEWSKQGEMGRRKLAQFTRYFTIVLG
FIQALGMSYGFNNLAGGMLIQNPGIGTYLLIAVVLTAGTAFLMWLGEQITAKGVGNGISI
IIFAGIVSGIPTILNQIYAQTFENVGEDLTLNIVRLLLVALAVVAVIVGVIYIQQAFRKI
PIQYAKRLEGRNPVGGHSTHLPLKVNPAGVIPVIFAVSFLIAPPTIASFFGTNDVTLWIR
RTFDYTHPVGMTIYVVLIIAFTYFYAFVQVNPEQMADNLKKQGGYIPGIRPGKNTQEYVT
RILYRLTLVGSLFLAFIAVLPVFFVNFANLPPSAQIGGTSLLIVVGVALETMKQLESQLV
KRHYRGFIK
Sequence of entity 3 (E), FASTA
>8YA0_3 Protein translocase subunit SecE (chains E)
QRVTNFFKEVVRELKKVSWPNRKELVNYTAVVLATVAFFTVFFAVIDLGISQLIRLVF
Sequence of entity 4 (V), FASTA
>8YA0_4 Nanobody (chains V)
QVQLVETGGGLVQPGGSLRLSCGASGSIFNMYAMGWYRQAPGKRREVVARIATDDSTMYP
DSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCYYQRTVMSQPYWGQGTQVTVS
Sequence of entity 5 (B), FASTA
>8YA0_5 Cell division protein FtsQ,Lactose permease (chains B)
AKKTILFLLTVLTTVLVSGWVVLGAQYEDGCSGVVILKTLHMFEVPFLLVGAFSNADTSI
SGDGDSPHSYHS
Sequence of entity 6 (C), FASTA
>8YA0_6 Nanobody (chains C)
VALVESGGALVQPGGSLRLSCAASGFPVNRYSMRWYRQAPGKEREWVAGMSSAGDRSSYE
DSVKGRFTISRDDARNTVYLQMNSLKPEDTAVYYCNVNVGFEYWGQGTQVTVS
Sequence of entity 7 (G), FASTA
>8YA0_7 Green fluorescent protein (chains G)
KGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVT
TFXVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGNYKTRAEVKFEGDTLVNRIE
LKGIDFKEDGNILGHKLEYNYNSHNVYITADKQKNGIKANFKIRHNIEDGSVQLADHYQQ
NTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGI
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| BEF | Beryllium trifluoride ion | Be F3 | 1 |
| MG | Magnesium ion | Mg | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Primary citation
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 P28366 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1TF5 2.18 Å, Crystal structure of SecA in an open conformation from Bacillus Subtilis
- 3JV2 2.5 Å, Crystal Structure of B. subtilis SecA with bound peptide
- 1M6N 2.7 Å, Crystal structure of the SecA translocation ATPase from Bacillus subtilis
- 1TF2 2.9 Å, Crystal structure of SecA:ADP in an open conformation from Bacillus Subtilis
- 1M74 3.0 Å, Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis
- 2IBM 3.2 Å, A novel dimer interface and conformational changes revealed by an X-ray structure of B.…
- 8Y9Y 3.29 Å, Structure of the SecA-SecY complex with the substrate FtsQ-LacY(+1C)
- 3IQY 3.3 Å, Active site mutants of B. subtilis SecA
- 7XHB 3.33 Å, Structure of the SecA/SecYE/proOmpA(4Y)-sfGFP complex with ADP
- 7XHA 3.35 Å, Structure of the SecA/SecYE/proOmpA(4Y)-sfGFP complex with ADP.BeF3-.
- 3IQM 3.4 Å, Active site mutants of B. subtilis SecA
- 8Y9Z 3.41 Å, Structure of the SecA-SecY complex with the substrate HmBRI-3TM
Browse structure collections
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