8PR5: Autoinhibited dynactin p150glued projection

Structure of the autoinhibited dynactin p150glued projection. Determined by electron microscopy at 8.6 Å resolution. Released 27 Mar 2024.

Method
Electron microscopy
Resolution
8.6 Å
Organism
Sus scrofa
Chains
2
Atoms
8,326
Mol. weight
190.89 kDa
Released
27 Mar 2024

Explore 8PR5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8PR5 contains 43 α-helices and 8 β-strands across 2 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: 20 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix215-349135
α-helix356-534179
α-helix554-59037
α-helix594-5974
α-helix602-63029
α-helix636-6383
α-helix645-67632
α-helix679-6879
α-helix689-6946
α-helix696-70712
α-helix718-73417
α-helix739-7402
α-helix742-77029
β-strand77111
α-helix7721
α-helix779-80325
β-strand816-81722
α-helix821-85232
β-strand86111
α-helix863-87816
α-helix885-90824
β-strand913-91422
α-helix915-9195
α-helix923-1048126
Chain B: 23 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix215-338124
α-helix339-3424
α-helix343-3475
α-helix354-535182
α-helix536-5383
α-helix555-59137
α-helix594-5974
α-helix602-63029
α-helix636-6383
α-helix645-67632
α-helix679-6879
α-helix689-6935
α-helix696-70712
α-helix718-73417
α-helix742-77029
β-strand77113
α-helix7721
α-helix779-80325
β-strand816-81724
α-helix821-85232
β-strand86113
α-helix863-87816
α-helix885-90824
β-strand913-91424
α-helix918-9203
α-helix9221
α-helix923-1048126

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Dynactin subunit 1A, Bprotein838Sus scrofaA0A287B8J2 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>8PR5_1 Dynactin subunit 1 (chains A, B)
SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ
RRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVD
ELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQK
LMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEK
VRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADY
QQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMEL
RQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLS
ENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMS
AHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFT
QSALDCMSVEVGRLRAFLQGGQEASDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGI
PAALAFGAQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKA
SEQIYGTPSSSPYECLRQSCNILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRA
EITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEK
VQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGIRGP

Primary citation

Molecular mechanism of dynein-dynactin complex assembly by LIS1. Singh, K., Lau, C.K., Manigrasso, G. et al. Science (2024) 383:eadk8544-eadk8544. DOI 10.1126/science.adk8544 · PubMed

Other PDB entries of the same protein (UniProt A0A287B8J2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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