8U6Y: Preholo-Proteasome from Beta 3 D205 deletion
Preholo-Proteasome from Beta 3 D205 deletion. Determined by electron microscopy at 2.8 Å resolution. Released 17 Apr 2024.
- Method
- Electron microscopy
- Resolution
- 2.8 Å
- Organism
- Saccharomyces cerevisiae S288C
- Chains
- 34
- Atoms
- 57,080
- Mol. weight
- 919.96 kDa
- Released
- 17 Apr 2024
Explore 8U6Y in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8U6Y contains 310 α-helices and 436 β-strands across 34 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.
Chains a and J: 5 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 11-16 | 6 | 5 |
| β-strand | 21-25 | 5 | 5 |
| β-strand | 43-45 | 3 | 6 |
| β-strand | 49-55 | 7 | 6 |
| α-helix | 57-78 | 22 | |
| α-helix | 81-83 | 3 | |
| α-helix | 84-97 | 14 | |
| β-strand | 105-112 | 8 | 6 |
| β-strand | 119-123 | 5 | 6 |
| β-strand | 124 | 1 | 7 |
| β-strand | 130 | 1 | 7 |
| β-strand | 136-140 | 5 | 5 |
| α-helix | 143-153 | 11 | |
| α-helix | 160-172 | 13 | |
| β-strand | 185-190 | 6 | 5 |
| β-strand | 195-200 | 6 | 5 |
Chains A and R: 10 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-15 | 4 | |
| α-helix | 18-20 | 3 | |
| α-helix | 26-34 | 9 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 50-56 | 7 | 1 |
| β-strand | 64 | 1 | 2 |
| β-strand | 72-74 | 3 | 3 |
| β-strand | 79-84 | 6 | 3 |
| α-helix | 87-108 | 22 | |
| α-helix | 111-113 | 3 | |
| α-helix | 114-130 | 17 | |
| β-strand | 131 | 1 | 4 |
| β-strand | 140-147 | 8 | 3 |
| β-strand | 151-157 | 7 | 3 |
| β-strand | 163-166 | 4 | 3 |
| β-strand | 169-171 | 3 | 1 |
| α-helix | 175-185 | 11 | |
| α-helix | 199-214 | 16 | |
| β-strand | 223-229 | 7 | 1 |
| β-strand | 233-235 | 3 | 1 |
| α-helix | 236-237 | 2 | |
| α-helix | 238-249 | 12 | |
Chains b and K: 6 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-8 | 5 | 13 |
| β-strand | 13-17 | 5 | 13 |
| β-strand | 35-39 | 5 | 14 |
| β-strand | 42-48 | 7 | 14 |
| α-helix | 52-71 | 20 | |
| α-helix | 74-76 | 3 | |
| α-helix | 77-93 | 17 | |
| α-helix | 96-99 | 4 | |
| β-strand | 100-108 | 9 | 14 |
| β-strand | 113-119 | 7 | 14 |
| β-strand | 125-127 | 3 | 14 |
| β-strand | 130-132 | 3 | 13 |
| α-helix | 144-146 | 3 | |
| α-helix | 154-171 | 18 | |
| β-strand | 180-185 | 6 | 13 |
| β-strand | 188-191 | 4 | 13 |
Chains B and S: 14 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12 | 1 | 8 |
| β-strand | 18 | 1 | 8 |
| α-helix | 19-30 | 12 | |
| α-helix | 32-33 | 2 | |
| β-strand | 34-38 | 5 | 9 |
| β-strand | 43-48 | 6 | 9 |
| β-strand | 56 | 1 | 3 |
| α-helix | 58-60 | 3 | |
| β-strand | 65-68 | 4 | 10 |
| β-strand | 71-77 | 7 | 10 |
| α-helix | 79-92 | 14 | |
| α-helix | 93-98 | 6 | |
| α-helix | 99-101 | 3 | |
| α-helix | 104-106 | 3 | |
| α-helix | 107-123 | 17 | |
| β-strand | 127 | 1 | 4 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-140 | 9 | 10 |
| β-strand | 144-150 | 7 | 10 |
| β-strand | 156-158 | 3 | 10 |
| β-strand | 159 | 1 | 11 |
| β-strand | 161-164 | 4 | 9 |
| α-helix | 168-178 | 11 | |
| α-helix | 185-199 | 15 | |
| β-strand | 209-214 | 6 | 9 |
| α-helix | 219-221 | 3 | |
| β-strand | 224-225 | 2 | 12 |
| β-strand | 235-237 | 3 | 9 |
| α-helix | 238-239 | 2 | |
| α-helix | 240-247 | 8 | |
Chains c and L: 9 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-8 | 7 | |
| α-helix | 23-28 | 6 | |
| α-helix | 35-38 | 4 | |
| β-strand | 44-45 | 2 | 108 |
| α-helix | 52-57 | 6 | |
| β-strand | 77-83 | 7 | 19 |
| β-strand | 86-89 | 4 | 19 |
| β-strand | 109-113 | 5 | 20 |
| β-strand | 116-119 | 4 | 20 |
| β-strand | 122 | 1 | 21 |
| α-helix | 124-145 | 22 | |
| α-helix | 148-150 | 3 | |
| α-helix | 151-164 | 14 | |
| β-strand | 172 | 1 | 21 |
| β-strand | 175-180 | 6 | 20 |
| β-strand | 184-190 | 7 | 20 |
| β-strand | 196-197 | 2 | 20 |
| β-strand | 201-205 | 5 | 19 |
| α-helix | 208-216 | 9 | |
| α-helix | 225-237 | 13 | |
| β-strand | 253-256 | 4 | 19 |
| β-strand | 259-262 | 4 | 19 |
Chains C and T: 11 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 20-29 | 10 | |
| α-helix | 33-34 | 2 | |
| β-strand | 35-40 | 6 | 15 |
| β-strand | 43-49 | 7 | 15 |
| β-strand | 57 | 1 | 11 |
| β-strand | 66-70 | 5 | 16 |
| β-strand | 73-79 | 7 | 16 |
| α-helix | 81-102 | 22 | |
| α-helix | 105-107 | 3 | |
| α-helix | 108-121 | 14 | |
| β-strand | 125 | 1 | 17 |
| α-helix | 129-131 | 3 | |
| β-strand | 133-141 | 9 | 16 |
| β-strand | 145-151 | 7 | 16 |
| β-strand | 157-159 | 3 | 16 |
| β-strand | 160 | 1 | 18 |
| β-strand | 162-165 | 4 | 15 |
| α-helix | 169-179 | 11 | |
| α-helix | 186-200 | 15 | |
| α-helix | 208-210 | 3 | |
| β-strand | 211-217 | 7 | 15 |
| β-strand | 226-229 | 4 | 15 |
| α-helix | 230-231 | 2 | |
| α-helix | 232-242 | 11 | |
Chains d and M: 5 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 30-35 | 6 | 25 |
| β-strand | 39-45 | 7 | 25 |
| β-strand | 48-50 | 3 | 26 |
| β-strand | 53-56 | 4 | 26 |
| β-strand | 63-66 | 4 | 27 |
| β-strand | 69-75 | 7 | 27 |
| α-helix | 77-97 | 21 | |
| α-helix | 105-117 | 13 | |
| β-strand | 126-133 | 8 | 27 |
| β-strand | 139-144 | 6 | 27 |
| β-strand | 150-153 | 4 | 27 |
| β-strand | 155-159 | 5 | 25 |
| α-helix | 162-172 | 11 | |
| α-helix | 188-190 | 3 | |
| α-helix | 196-213 | 18 | |
| β-strand | 214 | 1 | 54 |
| β-strand | 220-227 | 8 | 25 |
| β-strand | 230-237 | 8 | 25 |
Chains D and U: 10 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-12 | 3 | |
| α-helix | 18-28 | 11 | |
| α-helix | 31-32 | 2 | |
| β-strand | 33-37 | 5 | 22 |
| β-strand | 42-45 | 4 | 22 |
| β-strand | 55 | 1 | 18 |
| β-strand | 65-68 | 4 | 23 |
| β-strand | 71-77 | 7 | 23 |
| α-helix | 79-99 | 21 | |
| α-helix | 103-105 | 3 | |
| α-helix | 106-119 | 14 | |
| β-strand | 126 | 1 | 17 |
| α-helix | 127-129 | 3 | |
| β-strand | 131-137 | 7 | 23 |
| β-strand | 146-150 | 5 | 23 |
| β-strand | 156-158 | 3 | 23 |
| β-strand | 159 | 1 | 24 |
| β-strand | 161-164 | 4 | 22 |
| α-helix | 168-178 | 11 | |
| α-helix | 188-200 | 13 | |
| β-strand | 212-216 | 5 | 22 |
| β-strand | 220-223 | 4 | 22 |
| α-helix | 229-236 | 8 | |
9 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Proteasome subunit alpha type-1 | A, R | protein | 252 | Saccharomyces cerevisiae S288C | P21243 (AlphaFold model) |
| Proteasome subunit alpha type-2 | B, S | protein | 250 | Saccharomyces cerevisiae S288C | P23639 (AlphaFold model) |
| Proteasome subunit alpha type-3 | C, T | protein | 245 | Saccharomyces cerevisiae S288C | P23638 (AlphaFold model) |
| Proteasome subunit alpha type-4 | D, U | protein | 254 | Saccharomyces cerevisiae S288C | P40303 (AlphaFold model) |
| Proteasome subunit alpha type-5 | E, V | protein | 260 | Saccharomyces cerevisiae S288C | P32379 |
| Proteasome subunit alpha type-6 | F, W | protein | 234 | Saccharomyces cerevisiae S288C | P40302 |
| Proteasome subunit alpha type-7 | G, X | protein | 288 | Saccharomyces cerevisiae S288C | P21242 |
| Proteasome maturation factor UMP1 | H, Y | protein | 148 | Saccharomyces cerevisiae S288C | P38293 |
| Proteasome subunit beta type-2 | I, Z | protein | 261 | Saccharomyces cerevisiae S288C | P25043 |
| Proteasome subunit beta type-3 | J, a | protein | 204 | Saccharomyces cerevisiae S288C | P25451 |
| Proteasome subunit beta type-4 | K, b | protein | 198 | Saccharomyces cerevisiae S288C | P22141 |
| Proteasome subunit beta type-5 | L, c | protein | 287 | Saccharomyces cerevisiae S288C | P30656 |
5 more molecules are not listed.
Sequence of entity 1 (A, R), FASTA
>8U6Y_1 Proteasome subunit alpha type-1 (chains A, R)
MSGAAAASAAGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVP
DKLLDPTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKR
MANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITT
NLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAEN
IEERLVAIAEQD
Sequence of entity 2 (B, S), FASTA
>8U6Y_2 Proteasome subunit alpha type-2 (chains B, S)
MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSET
LSKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQE
ATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWN
DELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTS
QEINDRLEAL
Sequence of entity 3 (C, T), FASTA
>8U6Y_3 Proteasome subunit alpha type-3 (chains C, T)
MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQD
TSTEKLYKLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQ
GYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDY
KDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILV
KTGIT
Sequence of entity 4 (D, U), FASTA
>8U6Y_4 Proteasome subunit alpha type-4 (chains D, U)
MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRIT
PSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRY
TQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYD
RKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEK
QEQQEQDKKKKSNH
Sequence of entity 5 (E, V), FASTA
>8U6Y_5 Proteasome subunit alpha type-5 (chains E, V)
MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLE
SDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLA
LRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQ
AELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELI
KELKEKEAAESPEEADVEMS
Sequence of entity 6 (F, W), FASTA
>8U6Y_6 Proteasome subunit alpha type-6 (chains F, W)
MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQ
KKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNT
QSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFI
KIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
Sequence of entity 7 (G, X), FASTA
>8U6Y_7 Proteasome subunit alpha type-7 (chains G, X)
MTSIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLV
PQKNVKIQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYV
QAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLV
DHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAI
DFAQKEINGDDDEDEDDSDNVMSSDDENAPVATNANATTDQEGDIHLE
Sequence of entity 8 (H, Y), FASTA
>8U6Y_8 Proteasome maturation factor UMP1 (chains H, Y)
MNIVPQDTFKSQVSTDQDKSVLSSAVPSLPDTLRQQEGGAVPLSTQLNDRHPLESTLKNW
ETTQRQRQMEQYRQIFGIAEPMKRTMEMEIVNRTDFNPLSTNGSIHRDILLNKECSIDWE
DVYPGTGLQASTMVGDDVHSKIEKQLGI
Sequence of entity 9 (I, Z), FASTA
>8U6Y_9 Proteasome subunit beta type-2 (chains I, Z)
MAGLSFDNYQRNNFLAENSHTQPKATSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKNC
AKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQMLKQHLFKYQ
GHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEA
IKLASDAIQAGIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQKSYKFPRGTTA
VLKESIVNICDIQEEQVDITA
Sequence of entity 10 (J, a), FASTA
>8U6Y_10 Proteasome subunit beta type-3 (chains J, a)
MSDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDV
TTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPF
IAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQALLNAADRDAL
SGWGAVVYIIKKDEVVKRYLKMRQ
Sequence of entity 11 (K, b), FASTA
>8U6Y_11 Proteasome subunit beta type-4 (chains K, b)
MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYI
QANIQLYSIREDYELSPQAVSSFVRQELAKSIRSRRPYQVNVLIGGYDKKKNKPELYQID
YLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLLKLCVQELEKRMPMDFKGVI
VKIVDKDGIRQVDDFQAQ
Sequence of entity 12 (L, c), FASTA
>8U6Y_12 Proteasome subunit beta type-5 (chains L, c)
MQAIADSFSVPNRLVKELQYDNEQNLESDFVTGASQFQRLAPSLTVPPIASPQQFLRAHT
DDSRNPDCKIKIAHGTTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTM
AGGAADCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYT
RKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAA
HRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG
Primary citation
Mechanism of autocatalytic activation during proteasome assembly. Velez, B., Walsh Jr., R.M., Rawson, S. et al. Nat Struct Mol Biol (2024) 31:1167-1175. DOI 10.1038/s41594-024-01262-1 · PubMed
Other PDB entries of the same protein (UniProt P21243 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1RYP 1.9 Å, Crystal structure of the 20S proteasome from yeast at 2.4 Å resolution
- 8RVQ 2.02 Å, 20S proteasome from pre1-1
- 4R17 2.1 Å, Ligand-induced aziridine-formation at subunit beta5 of the yeast 20S proteasome
- 8RVL 2.14 Å, Proteasomal late precursor complex from pre1-1
- 8U7U 2.16 Å, Proteasome 20S Core Particle from Beta 3 D205 deletion
- 1G65 2.25 Å, Crystal structure of epoxomicin:20s proteasome reveals a molecular basis for selectivity…
- 8RVP 2.28 Å, Proteasomal late precursor complex from pre1-1, state 2
- 4QVP 2.3 Å, yCP beta5-M45T mutant in complex with bortezomib
- 5CZ4 2.3 Å, Yeast 20S proteasome at 2.3 A resolution
- 6HWE 2.3 Å, Yeast 20S proteasome beta2-G45A mutant in complex with carfilzomib
- 9GBK 2.39 Å, Blm10-20S proteasome complex from pre1-1
- 1G0U 2.4 Å, A gated channel into the proteasome core particle
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