6DV1: Alpha-E-catenin actin-binding domain

Crystal structure of the alpha-E-catenin actin-binding domain. Determined by X-ray diffraction at 2.2 Å resolution. Released 19 Dec 2018.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Mus musculus
Chains: 2
Atoms: 3,067
Mol. weight: 58.25 kDa
Released: 19 Dec 2018

Explore 6DV1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6DV1 contains 14 α-helices and 10 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: 6 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	664	1	1
β-strand	667	1	1
α-helix	669-675	7
α-helix	678-702	25
β-strand	705	1	2
α-helix	711-730	20
α-helix	739-765	27
α-helix	770-793	24
β-strand	799-803	5	3
β-strand	806-810	5	3
α-helix	812-840	29
β-strand	861	1	2

Chain B: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	649-651	3
β-strand	652-654	3	4
β-strand	664-666	3	4
α-helix	669-675	7
α-helix	678-703	26
α-helix	711-730	20
α-helix	739-765	27
α-helix	770-794	25
α-helix	796-798	3
β-strand	799-803	5	5
β-strand	806-810	5	5
α-helix	812-841	30

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Catenin alpha-1	A, B	protein	263	Mus musculus	P26231 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6DV1_1 Catenin alpha-1 (chains A, B)
GPLGSPEFSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVS
KWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTI
ADHCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELVVSGVDSAMSLIQAAK
NLMNAVVQTVKASYVASTKYQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIK
RASQKKHVNPVQALSEFKAMDSI

Primary citation

Force-dependent allostery of the alpha-catenin actin-binding domain controls adherens junction dynamics and functions. Ishiyama, N., Sarpal, R., Wood, M.N. et al. Nat Commun (2018) 9:5121-5121. DOI 10.1038/s41467-018-07481-7 · PubMed

Other PDB entries of the same protein (UniProt P26231 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1DOW 1.8 Å, Crystal structure of a chimera of beta-catenin and alpha-catenin
4E17 2.3 Å, Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin
4E18 2.4 Å, Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin
1L7C 2.5 Å, alpha-catenin fragment, residues 385-651
5Y04 2.85 Å, Crystal Structure of the complex between the vinculin D1 domain and alphaE-catenin
1DOV 3.0 Å, Crystal structure of the alpha-catenin dimerization domain
9DVA 3.1 Å, F-actin binding interface of alpha-E-catenin ABD (cadherin-catenin complex) and afadin
6WVT 3.56 Å, Structural basis of alphaE-catenin - F-actin catch bond behavior
6O3E 4.0 Å, mouse aE-catenin 82-883
4K1N 6.5 Å, Crystal structure of full-length mouse alphaE-catenin

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