8T08: Proteasome subunit alpha type-1
Preholo-Proteasome from Pre1-1 Pre4-1 Double Mutant. Determined by electron microscopy at 3.0 Å resolution. Released 6 Sept 2023.
- Method
- Electron microscopy
- Resolution
- 3.0 Å
- Organism
- Saccharomyces cerevisiae S288C
- Chains
- 34
- Atoms
- 55,104
- Mol. weight
- 919.94 kDa
- Released
- 6 Sept 2023
Explore 8T08 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8T08 contains 282 α-helices and 420 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, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-16 | 5 | 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 | 84-96 | 13 | |
| β-strand | 105-112 | 8 | 6 |
| β-strand | 119-123 | 5 | 6 |
| β-strand | 131 | 1 | 6 |
| β-strand | 136-139 | 4 | 5 |
| α-helix | 143-153 | 11 | |
| α-helix | 160-174 | 15 | |
| β-strand | 185-190 | 6 | 5 |
| β-strand | 195-200 | 6 | 5 |
Chains A and R: 9 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-15 | 4 | |
| α-helix | 26-34 | 9 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 51-56 | 6 | 1 |
| β-strand | 64 | 1 | 2 |
| α-helix | 66-68 | 3 | |
| β-strand | 72-73 | 2 | 3 |
| β-strand | 80-84 | 5 | 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 | 168-171 | 4 | 1 |
| α-helix | 175-185 | 11 | |
| α-helix | 199-214 | 16 | |
| β-strand | 223-228 | 6 | 1 |
| β-strand | 233-235 | 3 | 1 |
| α-helix | 238-249 | 12 | |
Chains b and K: 5 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-9 | 6 | 12 |
| β-strand | 12-17 | 6 | 12 |
| β-strand | 25-26 | 2 | 13 |
| β-strand | 35-39 | 5 | 14 |
| β-strand | 42-48 | 7 | 14 |
| α-helix | 52-71 | 20 | |
| α-helix | 77-92 | 16 | |
| β-strand | 100-108 | 9 | 14 |
| β-strand | 113-119 | 7 | 14 |
| β-strand | 125-127 | 3 | 14 |
| β-strand | 130-133 | 4 | 12 |
| α-helix | 134-137 | 4 | |
| α-helix | 140-147 | 8 | |
| α-helix | 154-171 | 18 | |
| β-strand | 180-185 | 6 | 12 |
| β-strand | 188-192 | 5 | 12 |
Chains B and S: 13 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12 | 1 | 7 |
| β-strand | 18 | 1 | 7 |
| α-helix | 19-30 | 12 | |
| α-helix | 32-33 | 2 | |
| β-strand | 34-39 | 6 | 8 |
| β-strand | 42-48 | 7 | 8 |
| β-strand | 56 | 1 | 3 |
| α-helix | 58-60 | 3 | |
| β-strand | 65-68 | 4 | 9 |
| β-strand | 71-77 | 7 | 9 |
| α-helix | 79-92 | 14 | |
| α-helix | 93-98 | 6 | |
| α-helix | 99-101 | 3 | |
| α-helix | 104-106 | 3 | |
| α-helix | 107-120 | 14 | |
| β-strand | 127 | 1 | 4 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-140 | 9 | 9 |
| β-strand | 144-150 | 7 | 9 |
| β-strand | 156-158 | 3 | 9 |
| β-strand | 159 | 1 | 10 |
| β-strand | 161-164 | 4 | 8 |
| α-helix | 168-177 | 10 | |
| α-helix | 185-199 | 15 | |
| β-strand | 209-214 | 6 | 8 |
| α-helix | 219-221 | 3 | |
| β-strand | 224-225 | 2 | 11 |
| β-strand | 235-238 | 4 | 8 |
| α-helix | 240-248 | 9 | |
Chains c and L: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 79-83 | 5 | 13 |
| β-strand | 86-90 | 5 | 13 |
| α-helix | 127-144 | 18 | |
| α-helix | 148-150 | 3 | |
| α-helix | 151-164 | 14 | |
| β-strand | 174-180 | 7 | 18 |
| β-strand | 184-190 | 7 | 18 |
| β-strand | 196-198 | 3 | 18 |
| β-strand | 201-203 | 3 | 13 |
| β-strand | 252-256 | 5 | 13 |
| β-strand | 259-262 | 4 | 13 |
Chains C and T: 10 helices, 12 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 | 10 |
| β-strand | 66-70 | 5 | 16 |
| β-strand | 73-79 | 7 | 16 |
| α-helix | 81-102 | 22 | |
| α-helix | 105-107 | 3 | |
| α-helix | 108-122 | 15 | |
| β-strand | 125 | 1 | 17 |
| β-strand | 133-139 | 7 | 16 |
| β-strand | 147-151 | 5 | 16 |
| β-strand | 157-160 | 4 | 16 |
| 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 | 23 |
| β-strand | 40-45 | 6 | 23 |
| β-strand | 48-50 | 3 | 24 |
| β-strand | 53-56 | 4 | 24 |
| β-strand | 63-66 | 4 | 25 |
| β-strand | 69-75 | 7 | 25 |
| α-helix | 77-97 | 21 | |
| α-helix | 101-104 | 4 | |
| α-helix | 105-117 | 13 | |
| β-strand | 126-133 | 8 | 25 |
| β-strand | 139-144 | 6 | 25 |
| β-strand | 150-152 | 3 | 25 |
| β-strand | 155-159 | 5 | 23 |
| α-helix | 162-173 | 12 | |
| α-helix | 199-213 | 15 | |
| β-strand | 214 | 1 | 50 |
| β-strand | 220-227 | 8 | 23 |
| β-strand | 230-237 | 8 | 23 |
Chains D and U: 10 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 18-28 | 11 | |
| α-helix | 31-32 | 2 | |
| β-strand | 33-37 | 5 | 19 |
| β-strand | 42-46 | 5 | 19 |
| β-strand | 55 | 1 | 16 |
| α-helix | 57-59 | 3 | |
| β-strand | 65 | 1 | 20 |
| β-strand | 71-77 | 7 | 20 |
| 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 | 131-138 | 8 | 20 |
| β-strand | 145-150 | 6 | 20 |
| β-strand | 156-158 | 3 | 20 |
| β-strand | 159 | 1 | 21 |
| β-strand | 161-164 | 4 | 19 |
| α-helix | 169-178 | 10 | |
| β-strand | 180 | 1 | 22 |
| β-strand | 183 | 1 | 22 |
| α-helix | 188-200 | 13 | |
| β-strand | 211-216 | 6 | 19 |
| β-strand | 220-223 | 4 | 19 |
| α-helix | 228-236 | 9 | |
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 | 258 | 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 | 205 | 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
>8T08_1 Proteasome subunit alpha type-1 (chains A, R)
MSGAAAASAAGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVP
DKLLDPTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKR
MANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITT
NLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAEN
IEERLVAIAEQD
Sequence of entity 2 (B, S), FASTA
>8T08_2 Proteasome subunit alpha type-2 (chains B, S)
MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSET
LSKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQE
ATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWN
DELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTS
QEINDRLEAL
Sequence of entity 3 (C, T), FASTA
>8T08_3 Proteasome subunit alpha type-3 (chains C, T)
MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQD
TSTEKLYKLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQ
GYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDY
KDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILV
KTGITKKDEDEEADEDMK
Sequence of entity 4 (D, U), FASTA
>8T08_4 Proteasome subunit alpha type-4 (chains D, U)
MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRIT
PSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRY
TQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYD
RKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEK
QEQQEQDKKKKSNH
Sequence of entity 5 (E, V), FASTA
>8T08_5 Proteasome subunit alpha type-5 (chains E, V)
MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLE
SDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLA
LRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQ
AELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELI
KELKEKEAAESPEEADVEMS
Sequence of entity 6 (F, W), FASTA
>8T08_6 Proteasome subunit alpha type-6 (chains F, W)
MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQ
KKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNT
QSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFI
KIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
Sequence of entity 7 (G, X), FASTA
>8T08_7 Proteasome subunit alpha type-7 (chains G, X)
MTSIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLV
PQKNVKIQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYV
QAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLV
DHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAI
DFAQKEINGDDDEDEDDSDNVMSSDDENAPVATNANATTDQEGDIHLE
Sequence of entity 8 (H, Y), FASTA
>8T08_8 Proteasome maturation factor UMP1 (chains H, Y)
MNIVPQDTFKSQVSTDQDKSVLSSAVPSLPDTLRQQEGGAVPLSTQLNDRHPLESTLKNW
ETTQRQRQMEQYRQIFGIAEPMKRTMEMEIVNRTDFNPLSTNGSIHRDILLNKECSIDWE
DVYPGTGLQASTMVGDDVHSKIEKQLGI
Sequence of entity 9 (I, Z), FASTA
>8T08_9 Proteasome subunit beta type-2 (chains I, Z)
MAGLSFDNYQRNNFLAENSHTQPKATSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKNC
AKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQMLKQHLFKYQ
GHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEA
IKLASDAIQAGIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQKSYKFPRGTTA
VLKESIVNICDIQEEQVDITA
Sequence of entity 10 (J, a), FASTA
>8T08_10 Proteasome subunit beta type-3 (chains J, a)
MSDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDV
TTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPF
IAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQALLNAADRDAL
SGWGAVVYIIKKDEVVKRYLKMRQD
Sequence of entity 11 (K, b), FASTA
>8T08_11 Proteasome subunit beta type-4 (chains K, b)
MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYI
QANIQLYSIREDYELSPQAVSSFVRQELAKSIRSRRPYQVNVLIGGYDKKKNKPELYQID
YLGTKVELPYGAHGYSGFYTFFLLDHHYRPDMTTEEGLDLLKLCVQELEKRMPMDFKGVI
VKIVDKDGIRQVDDFQAQ
Sequence of entity 12 (L, c), FASTA
>8T08_12 Proteasome subunit beta type-5 (chains L, c)
MQAIADSFSVPNRLVKELQYDNEQNLESDFVTGASQFQRLAPSLTVPPIASPQQFLRAHT
DDSRNPDCKIKIAHGTTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTM
AGGAADCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYT
RKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAA
HRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG
Primary citation
Structure of the preholoproteasome reveals late steps in proteasome core particle biogenesis. Walsh Jr., R.M., Rawson, S., Schnell, H.M. et al. Nat Struct Mol Biol (2023) 30:1516-1524. DOI 10.1038/s41594-023-01081-w · 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
Browse structure collections
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