6ITC: Protein translocase subunit SecA
Structure of a substrate engaged SecA-SecY protein translocation machine. Determined by electron microscopy at 3.45 Å resolution. Released 12 Jun 2019.
- Method
- Electron microscopy
- Resolution
- 3.45 Å
- Organisms
- Bacillus subtilis (strain 168), Geobacillus thermodenitrificans (strain NG80-2), Lama glama
- Chains
- 7
- Atoms
- 13,844
- Mol. weight
- 204.08 kDa
- Ligands
- BEF, MG, PGV, ADP
- Released
- 12 Jun 2019
Explore 6ITC in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6ITC contains 68 α-helices and 74 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: 40 helices, 27 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-29 | 15 | |
| α-helix | 30-32 | 3 | |
| α-helix | 41-52 | 12 | |
| α-helix | 62-77 | 16 | |
| α-helix | 84-93 | 10 | |
| β-strand | 97-99 | 3 | 1 |
| α-helix | 107-117 | 11 | |
| β-strand | 125-128 | 4 | 2 |
| α-helix | 131-146 | 16 | |
| β-strand | 153-154 | 2 | 2 |
| α-helix | 161-168 | 8 | |
| β-strand | 173-176 | 4 | 2 |
| α-helix | 177-187 | 11 | |
| α-helix | 193-195 | 3 | |
| α-helix | 198-199 | 2 | |
| α-helix | 201 | 1 | |
| β-strand | 204-206 | 3 | 2 |
| β-strand | 207 | 1 | 3 |
| α-helix | 209 | 1 | |
| α-helix | 210-215 | 6 | |
| β-strand | 220-226 | 7 | 4 |
| α-helix | 232-241 | 10 | |
| α-helix | 246-249 | 4 | |
| β-strand | 250-253 | 4 | 5 |
| β-strand | 258-261 | 4 | 5 |
| α-helix | 263-272 | 10 | |
| α-helix | 284-298 | 15 | |
| α-helix | 302-305 | 4 | |
| β-strand | 307-309 | 3 | 6 |
| β-strand | 312-314 | 3 | 6 |
| β-strand | 316 | 1 | 7 |
| β-strand | 323 | 1 | 7 |
| α-helix | 324 | 1 | |
| β-strand | 327-329 | 3 | 8 |
| α-helix | 334-340 | 7 | |
| β-strand | 349-356 | 8 | 4 |
| α-helix | 357-361 | 5 | |
| β-strand | 367 | 1 | 2 |
| β-strand | 370 | 1 | 3 |
| α-helix | 375-377 | 3 | |
| α-helix | 378-383 | 6 | |
| β-strand | 389-391 | 3 | 1 |
| β-strand | 400 | 1 | 9 |
| β-strand | 406-407 | 2 | 10 |
| α-helix | 411-426 | 16 | |
| β-strand | 432-435 | 4 | 11 |
| α-helix | 440-448 | 9 | |
| β-strand | 459 | 1 | 11 |
| α-helix | 464-466 | 3 | |
| α-helix | 467-470 | 4 | |
| α-helix | 471-473 | 3 | |
| β-strand | 480-483 | 4 | 11 |
| α-helix | 485-487 | 3 | |
| β-strand | 506-508 | 3 | 11 |
| α-helix | 516-524 | 9 | |
| β-strand | 533 | 1 | 9 |
| β-strand | 536 | 1 | 11 |
| β-strand | 538-539 | 2 | 10 |
| α-helix | 544-549 | 6 | |
| α-helix | 572-618 | 47 | |
| α-helix | 624-642 | 19 | |
| α-helix | 654-664 | 11 | |
| α-helix | 673-675 | 3 | |
| α-helix | 681-703 | 23 | |
| α-helix | 706-737 | 32 | |
| α-helix | 738-742 | 5 | |
| α-helix | 748-776 | 29 | |
Chain B: 2 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-19 | 17 | |
| α-helix | 20-23 | 4 | |
| β-strand | 54-56 | 3 | 8 |
| β-strand | 57 | 1 | 4 |
Chain C: 2 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 21 |
| β-strand | 11-12 | 2 | 22 |
| β-strand | 19-25 | 7 | 21 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 23 |
| β-strand | 47-51 | 5 | 23 |
| β-strand | 57-59 | 3 | 23 |
| β-strand | 68-72 | 5 | 21 |
| β-strand | 77-81 | 5 | 21 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 23 |
| β-strand | 98-102 | 3 | 23 |
| β-strand | 107-109 | 3 | 23 |
| β-strand | 110-111 | 2 | 22 |
Chain E: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-14 | 11 | |
| β-strand | 19 | 1 | 13 |
| α-helix | 23-58 | 36 | |
Chain G: 1 helix, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-22 | 11 | 19 |
| β-strand | 25-36 | 12 | 19 |
| β-strand | 41-48 | 8 | 19 |
| α-helix | 58-61 | 4 | |
| β-strand | 92-100 | 9 | 19 |
| β-strand | 105-115 | 11 | 19 |
| β-strand | 118-128 | 11 | 19 |
| β-strand | 141 | 1 | 20 |
| β-strand | 148-155 | 8 | 19 |
| β-strand | 160-170 | 11 | 19 |
| β-strand | 171 | 1 | 20 |
| β-strand | 176-187 | 12 | 19 |
| β-strand | 199-208 | 10 | 19 |
| β-strand | 217-227 | 11 | 19 |
Chain V: 1 helix, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 15 |
| β-strand | 11-12 | 2 | 16 |
| β-strand | 17-24 | 8 | 15 |
| β-strand | 34-37 | 4 | 17 |
| β-strand | 47-51 | 5 | 17 |
| β-strand | 58 | 1 | 17 |
| β-strand | 68-72 | 5 | 15 |
| β-strand | 77-83 | 7 | 15 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-94 | 4 | 17 |
| β-strand | 97 | 1 | 18 |
| β-strand | 106 | 1 | 18 |
| β-strand | 110-113 | 4 | 17 |
| β-strand | 114-115 | 2 | 16 |
Chain Y: 20 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-8 | 4 | |
| α-helix | 12-30 | 19 | |
| β-strand | 35 | 1 | 12 |
| α-helix | 36 | 1 | |
| α-helix | 41-46 | 6 | |
| β-strand | 68 | 1 | 12 |
| α-helix | 75-87 | 13 | |
| α-helix | 93-101 | 9 | |
| α-helix | 104-134 | 31 | |
| α-helix | 149-173 | 25 | |
| α-helix | 178-187 | 10 | |
| α-helix | 188-190 | 3 | |
| α-helix | 191-201 | 11 | |
| α-helix | 215-235 | 21 | |
| β-strand | 238-242 | 5 | 13 |
| β-strand | 244 | 1 | 14 |
| β-strand | 261-265 | 5 | 13 |
| α-helix | 272-288 | 17 | |
| α-helix | 295-303 | 9 | |
| α-helix | 311-330 | 20 | |
| α-helix | 333-342 | 10 | |
| β-strand | 346 | 1 | 14 |
| α-helix | 355-380 | 26 | |
| α-helix | 383-389 | 7 | |
| α-helix | 400-417 | 18 | |
| α-helix | 420-423 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein translocase subunit SecA | A | protein | 780 | Bacillus subtilis (strain 168) | P28366 (AlphaFold model) |
| Protein translocase subunit SecY | Y | protein | 424 | Geobacillus thermodenitrificans (strain NG80-2) | A4IJK8 (AlphaFold model) |
| Protein translocase subunit SecE | E | protein | 70 | Geobacillus thermodenitrificans (strain NG80-2) | A4IJH4 (AlphaFold model) |
| Nanobody | V | protein | 116 | Lama glama | |
| Translocating peptide | B | protein | 59 | Escherichia coli | P0A910 (AlphaFold model) |
| Green fluorescent protein | G | protein | 236 | Aequorea victoria | P42212 |
| Nanobody | C | protein | 112 | Lama glama | |
Sequence of entity 1 (A), FASTA
>6ITC_1 Protein translocase subunit SecA (chains A)
MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD
LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT
GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL
GFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAF
VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM
QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY
FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE
DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV
TIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS
MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD
DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL
INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV
DSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKAEI
Sequence of entity 2 (Y), FASTA
>6ITC_2 Protein translocase subunit SecY (chains Y)
MFRTISNFMRVSDIRNKIIFTLLMLIVFRIGTFIPVPSVNTDVLKLQDQLNAFGVLNIFC
GGALQNFSIFAMGVMPYITASIIVQLLQMDVVPKFAEWSKQGEMGRRKLAQFTRYFTIVL
GFIQALGMSYGFNNLAGGMLIQNPGIGTYLLIAVVLTAGTAFLMWLGEQITAKGVGNGIS
IIIFAGIVSGIPTILNQIYAQTFGGLNIVRLLLVALAVVAVIVGVIYIQQAFRKIPIQYA
KRLEGRNPVGGHSTHLPLKVNPAGVIPVIFAVSFLIAPPTIASFFGTNDVTLWIRRTFDY
THPVGMTIYVVLIIAFTYFYAFVQVNPEQMADNLKKQGGYIPGIRPGKNTQEYVTRILYR
LTLVGSLFLAFIAVLPVFFVNFANLPPSAQIGGTSLLIVVGVALETMKQLESQLVKRHYR
GFIK
Sequence of entity 3 (E), FASTA
>6ITC_3 Protein translocase subunit SecE (chains E)
MQRVTNFFKEVVRELKKVSWPNRKELVNYTAVVLATVAFFTVFFAVIDLGISQLIRLVFE
GGHHHHHHHH
Sequence of entity 4 (V), FASTA
>6ITC_4 Nanobody (chains V)
QVQLVETGGGLVQPGGSLRLSCGASGSIFNMYAMGWYRQAPGKRREVVARIATDDSTMYP
DSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCYYQRTVMSQPYWGQGTQVTVS
Sequence of entity 5 (B), FASTA
>6ITC_5 Translocating peptide (chains B)
MAKKTAIAIAVALAGFATVASYAQYEDGCSGELERQHTFAGGARSISGDGDSPHSYHSG
Sequence of entity 6 (G), FASTA
>6ITC_6 Green fluorescent protein (chains G)
MSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTL
VTTFXVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGNYKTRAEVKFEGDTLVNR
IELKGIDFKEDGNILGHKLEYNYNSHNVYITADKQKNGIKANFKIRHNIEDGSVQLADHY
QQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITHGMDELYK
Sequence of entity 7 (C), FASTA
>6ITC_7 Nanobody (chains C)
VALVESGGALVQPGGSLRLSCAASGFPVNRYSMRWYRQAPGKEREWVAGMSAGDRSSYED
SVKGRFTISRDDARNTVYLQMNSLKPEDTAVYYCNVNVGFEYWGQGTQVTVS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| BEF | Beryllium trifluoride ion | Be F3 | 1 |
| MG | Magnesium ion | Mg | 1 |
| PGV | (1R)-2-{[{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(palmitoylo… | C40 H77 O10 P | 2 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Primary citation
Structure of the substrate-engaged SecA-SecY protein translocation machine. Ma, C., Wu, X., Sun, D. et al. Nat Commun (2019) 10:2872-2872. DOI 10.1038/s41467-019-10918-2 · 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
- 8YA0 2.97 Å, Structure of the SecA-SecY complex with the substrate FtsQ-LacY(+7C)
- 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
Browse structure collections
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