4E17: Vinculin

Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin. Determined by X-ray diffraction at 2.3 Å resolution. Released 16 May 2012.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Gallus gallus, Mus musculus
Chains: 2
Atoms: 2,223
Mol. weight: 33.78 kDa
Released: 16 May 2012

Explore 4E17 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4E17 contains 11 α-helices and 2 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: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	0-4	5
β-strand	6	1	1
α-helix	7-28	22
α-helix	41-63	23
α-helix	68-73	6
α-helix	75-97	23
α-helix	102-145	44
α-helix	146-149	4
α-helix	154-179	26
β-strand	182	1	1
α-helix	185-215	31
α-helix	223-248	26

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	328-352	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vinculin	A	protein	263	Gallus gallus	P12003 (AlphaFold model)
Catenin alpha-1	B	protein	40	Mus musculus	P26231 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4E17_1 Vinculin (chains A)
GGIQMPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVSAVQAAVSNLVR
VGKETVQTTEDQILKRDMPPAFIKVENACTKLVRAAQMLQADPYSVPARDYLIDGSRGIL
SGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMID
ERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNTKSQGIEEALKNRNFTVEK
MSAEINEIIRVLQLTSWDEDAWA

Sequence of entity 2 (B), FASTA

>4E17_2 Catenin alpha-1 (chains B)
GGIQDSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAG

Primary citation

Conformational plasticity of alpha-catenin revealed by binding interactions with vinculin. Choi, H.-J., Pokutta, S., Bankston, L. et al. To be published.

Other PDB entries of the same protein (UniProt P12003 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1QKR 1.8 Å, Crystal structure of the vinculin tail and a pathway for activation
1ZVZ 1.8 Å, Vinculin Head (0-258) in Complex with the Talin Rod Residue 820-844
1T01 2.06 Å, Vinculin complexed with the VBS1 helix from talin
1ZW2 2.1 Å, Vinculin Head (0-258) in Complex with the Talin Rod residues 2345-2369
3ZDL 2.3 Å, Vinculin head (1-258) in complex with a RIAM fragment
1U6H 2.38 Å, Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)
4E18 2.4 Å, Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin
1XWJ 2.6 Å, Vinculin head (1-258) in complex with the talin vinculin binding site 3 (1945-1969)
2GDC 2.74 Å, Structure of Vinculin VD1 / IpaA560-633 complex
6FQ4 2.89 Å, Structure of Chlamydial virulence factor TarP and vinculin head domain
6NR7 3.0 Å, Rerefinement of chicken vinculin
1ST6 3.1 Å, Crystal structure of a cytoskeletal protein

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