6WVT: AlphaE-catenin - F-actin catch bond behavior

Structural basis of alphaE-catenin - F-actin catch bond behavior. Determined by electron microscopy at 3.56 Å resolution. Released 7 Oct 2020.

Method: Electron microscopy
Resolution: 3.56 Å
Organisms: Oryctolagus cuniculus, Mus musculus
Chains: 12
Atoms: 25,248
Mol. weight: 411.36 kDa
Ligands: ADP, MG
Released: 7 Oct 2020

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

Secondary structure: helices and β-sheets

6WVT contains 168 α-helices and 108 β-strands across 12 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 B, D, E, F, H and I: 23 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	17-21	5	1
β-strand	29-31	3	1
β-strand	35-38	4	2
β-strand	53-54	2	2
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	2
β-strand	71-72	2	3
β-strand	75-76	2	3
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-125	13
β-strand	131-136	6	1
α-helix	139-144	6
β-strand	150-155	6	4
β-strand	160-165	6	4
β-strand	170	1	4
α-helix	172-174	3
β-strand	176-178	3	4
α-helix	182-192	11
α-helix	205-215	11
α-helix	223-229	7
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-256	4
α-helix	258-261	4
α-helix	276-282	7
α-helix	290-294	5
β-strand	297-298	2	4
α-helix	302-304	3
α-helix	309-317	9
α-helix	335-337	3
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	1
α-helix	359-362	4
α-helix	366-370	5
α-helix	371-374	4

Chains K, L, N, O, Q and X: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	713-726	14
α-helix	740-763	24
α-helix	770-801	32
α-helix	813-842	30
α-helix	865-868	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	B, D, E, F, H, I	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)
Catenin alpha-1	K, L, N, O, Q, X	protein	236	Mus musculus	P26231 (AlphaFold model)

Sequence of entity 1 (B, D, E, F, H, I), FASTA

>6WVT_1 Actin, alpha skeletal muscle (chains B, D, E, F, H, I)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (K, L, N, O, Q, X), FASTA

>6WVT_2 Catenin alpha-1 (chains K, L, N, O, Q, X)
AIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFT
RGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQL
NICSKVKAEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMA
SLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	6
MG	Magnesium ion	Mg	6

Primary citation

Structural basis of alpha E-catenin-F-actin catch bond behavior. Xu, X.P., Pokutta, S., Torres, M. et al. Elife (2020) 9. DOI 10.7554/eLife.60878 · PubMed

Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4B1Y 1.29 Å, Structure of the Phactr1 RPEL-3 bound to G-actin
2FXU 1.35 Å, X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
4K41 1.4 Å, Crystal structure of actin in complex with marine macrolide kabiramide C
1QZ5 1.45 Å, Structure of rabbit actin in complex with kabiramide C
1WUA 1.45 Å, The structure of Aplyronine A-actin complex
2Q0U 1.45 Å, Structure of Pectenotoxin-2 and Latrunculin B Bound to Actin
2V52 1.45 Å, Structure of MAL-RPEL2 complexed to G-actin
3MN5 1.5 Å, Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation
2PBD 1.5 Å, Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
5ZZA 1.53 Å, OdinProfilin/Rabbit Actin Complex
1J6Z 1.54 Å, Uncomplexed actin
1QZ6 1.6 Å, Structure of rabbit actin in complex with jaspisamide A

Browse structure collections

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