8I6V: Vacuolar transporter chaperone complex subunit 1
Cryo-EM structure of the polyphosphate polymerase VTC complex(Vtc4/Vtc3/Vtc1). Determined by electron microscopy at 3.06 Å resolution. Released 1 Mar 2023.
- Method
- Electron microscopy
- Resolution
- 3.06 Å
- Organism
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
- Chains
- 5
- Atoms
- 13,172
- Mol. weight
- 224.48 kDa
- Ligands
- MN, 3PO, PO4, POV
- Released
- 1 Mar 2023
Explore 8I6V in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8I6V contains 67 α-helices and 25 β-strands across 5 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: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-52 | 30 | |
| α-helix | 56-83 | 28 | |
| α-helix | 100-121 | 22 | |
Chain B: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-51 | 29 | |
| α-helix | 56-86 | 31 | |
| α-helix | 100-121 | 22 | |
Chain C: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-52 | 30 | |
| α-helix | 56-88 | 33 | |
| α-helix | 99-120 | 22 | |
Chain D: 32 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-9 | 7 | |
| α-helix | 13-15 | 3 | |
| α-helix | 22-28 | 7 | |
| α-helix | 31-35 | 5 | |
| α-helix | 46-86 | 41 | |
| α-helix | 96-133 | 38 | |
| α-helix | 139-140 | 2 | |
| α-helix | 142-150 | 9 | |
| α-helix | 160-161 | 2 | |
| α-helix | 162-173 | 12 | |
| α-helix | 174-178 | 5 | |
| α-helix | 188-194 | 7 | |
| β-strand | 205-212 | 8 | 1 |
| α-helix | 217-225 | 9 | |
| β-strand | 231-233 | 3 | 2 |
| α-helix | 235-237 | 3 | |
| β-strand | 246-247 | 2 | 2 |
| α-helix | 294-295 | 2 | |
| β-strand | 296-302 | 7 | 1 |
| α-helix | 307-313 | 7 | |
| β-strand | 320-327 | 8 | 1 |
| α-helix | 330-332 | 3 | |
| β-strand | 336-344 | 9 | 1 |
| β-strand | 353-361 | 9 | 1 |
| α-helix | 366-370 | 5 | |
| α-helix | 376-388 | 13 | |
| α-helix | 392-412 | 21 | |
| β-strand | 415-427 | 13 | 1 |
| β-strand | 435-447 | 13 | 1 |
| α-helix | 475-478 | 4 | |
| α-helix | 479-480 | 2 | |
| β-strand | 484-486 | 3 | 1 |
| β-strand | 490-497 | 8 | 1 |
| α-helix | 508-514 | 7 | |
| β-strand | 519-521 | 3 | 1 |
| α-helix | 527-536 | 10 | |
| α-helix | 551-553 | 3 | |
| α-helix | 561-583 | 23 | |
| α-helix | 584-588 | 5 | |
| α-helix | 697-725 | 29 | |
| α-helix | 728-730 | 3 | |
| α-helix | 734-766 | 33 | |
| α-helix | 778-804 | 27 | |
| α-helix | 823-833 | 11 | |
Chain E: 26 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-8 | 6 | |
| α-helix | 13-15 | 3 | |
| α-helix | 22-36 | 15 | |
| α-helix | 42-86 | 45 | |
| α-helix | 98-137 | 40 | |
| α-helix | 143-152 | 10 | |
| α-helix | 161-177 | 17 | |
| β-strand | 194-203 | 10 | 2 |
| α-helix | 205-207 | 3 | |
| α-helix | 208-216 | 9 | |
| β-strand | 221-223 | 3 | 2 |
| β-strand | 236-243 | 8 | 2 |
| α-helix | 248-254 | 7 | |
| β-strand | 260-268 | 9 | 2 |
| β-strand | 275-283 | 9 | 2 |
| β-strand | 293-300 | 8 | 2 |
| α-helix | 301-303 | 3 | |
| α-helix | 304-309 | 6 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-324 | 6 | |
| α-helix | 329-349 | 21 | |
| β-strand | 352-366 | 15 | 2 |
| β-strand | 369-384 | 16 | 2 |
| α-helix | 414-416 | 3 | |
| β-strand | 417-419 | 3 | 2 |
| β-strand | 423-432 | 10 | 2 |
| α-helix | 436-438 | 3 | |
| α-helix | 439-445 | 7 | |
| β-strand | 450-452 | 3 | 2 |
| α-helix | 458-466 | 9 | |
| β-strand | 473-474 | 2 | 3 |
| α-helix | 479-482 | 4 | |
| α-helix | 511-523 | 13 | |
| α-helix | 607-608 | 2 | |
| β-strand | 612-613 | 2 | 3 |
| α-helix | 624-647 | 24 | |
| α-helix | 654-656 | 3 | |
| α-helix | 657-686 | 30 | |
| α-helix | 698-717 | 20 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Vacuolar transporter chaperone complex subunit 1 | A, B, C | protein | 129 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40046 (AlphaFold model) |
| Vacuolar transporter chaperone 3 complex subunit 3 | D | protein | 835 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q02725 (AlphaFold model) |
| Vacuolar transporter chaperone complex subunit 4 | E | protein | 721 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P47075 (AlphaFold model) |
Sequence of entity 1 (A, B, C), FASTA
>8I6V_1 Vacuolar transporter chaperone complex subunit 1 (chains A, B, C)
MSSAPLLQRTPGKKIALPTRVEPKVFFANERTFLSWLNFTVMLGGLGVGLLNFGDKIGRV
SAGLFTFVAMGTMIYALVTYHWRAAAIRRRGSGPYDDRLGPTLLCFFLLVAVIINFILRL
KYNDANTKL
Sequence of entity 2 (D), FASTA
>8I6V_2 Vacuolar transporter chaperone 3 complex subunit 3 (chains D)
MLFGIKLANDVYPPWKDSYIDYERLKKLLKESVIHDGRSSVDSWSERNESDFVEALDKEL
EKVYTFQISKYNAVLRKLDDLEENTKSAEKIQKINSEQFKNTLEECLDEAQRLDNFDRLN
FTGFIKIVKKHDKLHPNYPSVKSLLQVRLKELPFNNSEEYSPLLYRISYLYEFLRSNYDH
PNTVSKSLASTSKLSHFSNLEDASFKSYKFWVHDDNIMEVKARILRHLPALVYASVPNEN
DDFVDNLESDVRVQPEARLNIGSKSNSLSSDGNSNQDVEIGKSKSVIFPQSYDPTITTLY
FDNDFFDLYNNRLLKISGAPTLRLRWIGKLLDKPDIFLEKRTFTENTETGNSSFEEIRLQ
MKAKFINNFIFKNDPSYKNYLINQLRERGTQKEELEKLSRDFDNIQNFIVEEKLQPVLRA
TYNRTAFQIPGDQSIRVTIDSNIMYIREDSLDKNRPIRNPENWHRDDIDSNIPNPLRFLR
AGEYSKFPYSVMEIKVINQDNSQMPNYEWIKDLTNSHLVNEVPKFSLYLQGVASLFGEDD
KYVNILPFWLPDLETDIRKNPQEAYEEEKKTLQKQKSIHDKLDNMRRLSKISVPDGKTTE
RQGQKDQNTRHVIADLEDHESSDEEGTALPKKSAVKKGKKFKTNAAFLKILAGKNISENG
NDPYSDDTDSASSFQLPPGVKKPVHLLKNAGPVKVEAKVWLANERTFNRWLSVTTLLSVL
TFSIYNSVQKAEFPQLADLLAYVYFFLTLFCGVWAYRTYLKRLTLIKGRSGKHLDAPVGP
ILVAVVLIVTLVVNFSVAFKEAARRERGLVNVSSQPSLPRTLKPIQDFIFNLVGE
Sequence of entity 3 (E), FASTA
>8I6V_3 Vacuolar transporter chaperone complex subunit 4 (chains E)
MKFGEHLSKSLIRQYSYYYISYDDLKTELEDNLSKNNGQWTQELETDFLESLEIELDKVY
TFCKVKHSEVFRRVKEVQEQVQHTVRLLDSNNPPTQLDFEILEEELSDIIADVHDLAKFS
RLNYTGFQKIIKKHDKKTGFILKPVFQVRLDSKPFFKENYDELVVKISQLYDIARTSGRP
IKGDSSAGGKQQNFVRQTTKYWVHPDNITELKLIILKHLPVLVFNTNKEFEREDSAITSI
YFDNENLDLYYGRLRKDEGAEAHRLRWYGGMSTDTIFVERKTHREDWTGEKSVKARFALK
ERHVNDFLKGKYTVDQVFAKMRKEGKKPMNEIENLEALASEIQYVMLKKKLRPVVRSFYN
RTAFQLPGDARVRISLDTELTMVREDNFDGVDRTHKNWRRTDIGVDWPFKQLDDKDICRF
PYAVLEVKLQTQLGQEPPEWVRELVGSHLVEPVPKFSKFIHGVATLLNDKVDSIPFWLPQ
MDVDIRKPPLPTNIEITRPGRSDNEDNDFDEDDEDDAALVAAMTNAPGNSLDIEESVGYG
ATSAPTSNTNHVVESANAAYYQRKIRNAENPISKKYYEIVAFFDHYFNGDQISKIPKGTT
FDTQIRAPPGKTICVPVRVEPKVYFATERTYLSWLSISILLGGVSTTLLTYGSPTAMIGS
IGFFITSLAVLIRTVMVYAKRVVNIRLKRAVDYEDKIGPGMVSVFLILSILFSFFCNLVA
K
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MN | Manganese (II) ion | Mn | 1 |
| 3PO | Triphosphate | H5 O10 P3 | 1 |
| PO4 | Phosphate ion | O4 P | 3 |
| POV | (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl… | C42 H82 N O8 P | 1 |
Primary citation
Cryo-EM structure of the polyphosphate polymerase VTC reveals coupling of polymer synthesis to membrane transit. Liu, W., Wang, J., Comte-Miserez, V. et al. EMBO J (2023) 42:e113320-e113320. DOI 10.15252/embj.2022113320 · PubMed
Other PDB entries of the same protein (UniProt P40046 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7YTJ 3.0 Å, Cryo-EM structure of VTC complex
- 9UMG 3.04 Å, Cryo-EM structure of VTC complex(Vtc5/Vtc4/Vtc3/Vtc1)
Browse structure collections
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