6TZ4: Charged multivesicular body protein 1b

CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (right-handed). Determined by electron microscopy at 3.2 Å resolution. Released 8 Apr 2020.

Method: Electron microscopy
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 72
Atoms: 99,216
Mol. weight: 1573.73 kDa
Released: 8 Apr 2020

Explore 6TZ4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6TZ4 contains 540 α-helices and 0 β-strands across 72 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 01, AA, AB, B, CA, CB, D, EA, EB, F, GA, GB, H, IA, IB, J, KA, KB, L, MA, MB, N, OA, OB, P, QA, QB, R, SA, SB, T, UA, W, WA, Y and YA: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	8-44	37
α-helix	50-81	32
α-helix	83-86	4
α-helix	94-110	17
α-helix	116-127	12
α-helix	136-140	5
α-helix	146-151	6
α-helix	156-158	3
α-helix	159-172	14
α-helix	181-185	5

Chains 02, A, BA, BB, C, DA, DB, E, FA, FB, G, HA, HB, I, JA, JB, K, LA, LB, M, NA, NB, O, PA, PB, Q, RA, RB, S, TA, V, VA, X, XA, Z and ZA: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	3-40	38
α-helix	45-105	61
α-helix	108-139	32
α-helix	146-160	15
α-helix	187-197	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Charged multivesicular body protein 1b	02, A, BA, BB, C, DA, DB, E, FA, FB, G, HA, HB, I, JA, JB, K, LA, LB, M, NA, NB, O, PA, PB, Q, RA, RB, S, TA, V, VA, X, XA, Z, ZA	protein	199	Homo sapiens	Q7LBR1 (AlphaFold model)
IST1 homolog	01, AA, AB, B, CA, CB, D, EA, EB, F, GA, GB, H, IA, IB, J, KA, KB, L, MA, MB, N, OA, OB, P, QA, QB, R, SA, SB, T, UA, W, WA, Y, YA	protein	189	Homo sapiens	P53990 (AlphaFold model)

Sequence of entity 1 (02, A, BA, BB, C, DA, DB, E, FA, FB, G, HA, HB, I, JA, JB, K, LA, LB, M, NA, NB, O, PA, PB, Q, RA, RB, S, TA, V, VA, X, XA, Z, ZA), FASTA

>6TZ4_1 Charged multivesicular body protein 1b (chains 02, A, BA, BB, C, DA, DB, E, FA, FB, G, HA, HB, I, JA, JB, K, LA, LB, M, NA, NB, O, PA, PB, Q, RA, RB, S, TA, V, VA, X, XA, Z, ZA)
MSNMEKHLFNLKFAAKELSRSAKKCDKEEKAEKAKIEKAIQKGNMEVARIHAENAIRQKN
QAVNFLRMSARVDAVAARVQTAVTMGKVTKSMAGVVKSMDATLKTMNLEKISALMDKFEH
QFETLDVQTQQMEDTMSSTTTLTTPQNQVDMLLQEMADEAGLDLNMELPQGQTGSVGTSV
ASAEQDELSQRLARLRDQV

Sequence of entity 2 (01, AA, AB, B, CA, CB, D, EA, EB, F, GA, GB, H, IA, IB, J, KA, KB, L, MA, MB, N, OA, OB, P, QA, QB, R, SA, SB, T, UA, W, WA, Y, YA), FASTA

>6TZ4_2 IST1 homolog (chains 01, AA, AB, B, CA, CB, D, EA, EB, F, GA, GB, H, IA, IB, J, KA, KB, L, MA, MB, N, OA, OB, P, QA, QB, R, SA, SB, T, UA, W, WA, Y, YA)
MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHII
REDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIV
ADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPD
SVVMAEAPP

Primary citation

Membrane constriction and thinning by sequential ESCRT-III polymerization. Nguyen, H.C., Talledge, N., McCullough, J. et al. Nat Struct Mol Biol (2020) 27:392-399. DOI 10.1038/s41594-020-0404-x · PubMed

Other PDB entries of the same protein (UniProt Q7LBR1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4TXR 1.0 Å, Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM and CHMP5 MIM
4TXQ 2.21 Å, Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM
3EAB 2.5 Å, Crystal structure of Spastin MIT in complex with ESCRT III
8V2S 2.72 Å, CHMP1B/IST1 dsDNA bound copolymer
6E8G 2.9 Å, CryoEM reconstruction of IST1-CHMP1B copolymer filament bound to ssDNA at 2.9 Angstrom…
8V2Q 2.95 Å, CHMP1B/IST1 ssRNA bound copolymer
8V2R 3.01 Å, CHMP1B/IST1 ssDNA bound copolymer
6TZ5 3.1 Å, CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1…
3JC1 4.0 Å, Electron cryo-microscopy of the IST1-CHMP1B ESCRT-III copolymer
6TZ9 6.2 Å, CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B only

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