8S32: GroEL with bound GroTAC peptide

GroEL with bound GroTAC peptide. Determined by electron microscopy at 2.45 Å resolution. Released 28 Feb 2024.

Method: Electron microscopy
Resolution: 2.45 Å
Organisms: Escherichia coli, synthetic construct
Chains: 28
Atoms: 55,552
Mol. weight: 847.96 kDa
Released: 28 Feb 2024

Explore 8S32 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8S32 contains 322 α-helices and 364 β-strands across 28 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 1, 2, O, P, Q, R, S, T, U, V, W, X, Y and Z: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	19-20	2	9
β-strand	26-27	2	9

Chains A, B, C, D, E, F, G, H, I, J, K, L, M and N: 23 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
α-helix	9-27	19
α-helix	34-35	2
β-strand	36-39	4	2
α-helix	46	1
β-strand	47-49	3	2
α-helix	52-58	7
α-helix	64-84	21
α-helix	88-108	21
α-helix	112-133	22
β-strand	135	1	3
α-helix	140-150	11
α-helix	155-168	14
β-strand	173-178	6	4
β-strand	185-189	5	4
β-strand	192-194	3	5
β-strand	198	1	6
α-helix	201-203	3
β-strand	206	1	7
β-strand	211	1	7
β-strand	212-215	4	5
β-strand	218-222	5	6
α-helix	229-242	14
β-strand	246-250	5	6
α-helix	258-267	10
β-strand	273-276	4	6
α-helix	277	1
α-helix	282-295	14
β-strand	300	1	6
α-helix	308-310	3
β-strand	317-318	2	6
β-strand	319-324	6	5
β-strand	329-334	6	5
α-helix	338-353	16
α-helix	358-373	16
β-strand	375-380	6	4
α-helix	385-408	24
β-strand	410-412	3	3
α-helix	416-424	9
α-helix	433-445	13
α-helix	448-457	10
α-helix	461-470	10
β-strand	475-478	4	8
β-strand	483-486	4	8
β-strand	493-495	3	3
α-helix	496-514	19
β-strand	516-522	7	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chaperonin GroEL	A, B, C, D, E, F, G, H, I, J, K, L, M, N	protein	548	Escherichia coli	P0A6F5 (AlphaFold model)
GroTAC	1, 2, O, P, Q, R, S, T, U, V, W, X, Y, Z	protein	28	synthetic construct

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N), FASTA

>8S32_1 Chaperonin GroEL (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N)
MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREI
ELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGI
DKAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDG
TGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAV
AKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTV
ISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDY
DREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALI
RVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNA
ATEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGG
MGGMGGMM

Sequence of entity 2 (1, 2, O, P, Q, R, S, T, U, V, W, X, Y, Z), FASTA

>8S32_2 GroTAC (chains 1, 2, O, P, Q, R, S, T, U, V, W, X, Y, Z)
CYRGGRPALRVVKXXXSWMTTPWGFHLP

Primary citation

Targeted protein degradation in Escherichia coli using CLIPPERs. Izert-Nowakowska, M.A., Klimecka, M.M., Antosiewicz, A. et al. EMBO Rep (2025) 26:3994-4016. DOI 10.1038/s44319-025-00510-9 · PubMed

Other PDB entries of the same protein (UniProt P0A6F5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3VZ6 1.5 Å, Crystal Structure Analysis of the Mini-chaperonines, variant with Gly 184 replaced with…
1KID 1.7 Å, Groel (HSP60 class) fragment (apical domain) comprising residues 191-376, mutant with…
3VZ7 1.8 Å, Crystal Structure Analysis of the mini-chaperonin variant with Pro 187 Gly
3VZ8 1.9 Å, Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro…
1KP8 2.0 Å, Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of…
1SX3 2.0 Å, GroEL14-(ATPgammaS)14
1DK7 2.02 Å, Crystal structure of an isolated apical domain of groel
1LA1 2.06 Å, Gro-EL Fragment (Apical Domain) Comprising Residues 188-379
1DKD 2.1 Å, Crystal structure of a groel (apical domain) and a dodecameric peptide complex
1FY9 2.2 Å, Crystal structure of the hexa-substituted mutant of the molecular chaperonin groel…
1FYA 2.2 Å, Crystal structure of the hexa-substituted mutant of the molecular chaperonin groel…
8BKZ 2.3 Å, GroEL:GroES-ATP complex under continuous turnover conditions

Browse structure collections

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