2YJE: Oligomeric assembly of actin

Oligomeric assembly of actin bound to MRTF-A. Determined by X-ray diffraction at 3.1 Å resolution. Released 6 Jul 2011.

Method: X-ray diffraction
Resolution: 3.1 Å
Organisms: ORYCTOLAGUS CUNICULUS, MUS MUSCULUS
Chains: 4
Atoms: 8,199
Mol. weight: 144.85 kDa
Ligands: LAB, ATP, MG
Released: 6 Jul 2011

Explore 2YJE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2YJE contains 75 α-helices and 53 β-strands across 4 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: 23 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	29-32	4	1
β-strand	71-72	2	2
β-strand	75-76	2	2
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	150-155	6	3
β-strand	160-166	7	3
β-strand	169-170	2	3
α-helix	172-174	3
β-strand	176-178	3	3
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	4
β-strand	247-250	4	4
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	3
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	3
α-helix	333-337	5
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-370	4

Chain B: 25 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	5
β-strand	16-21	6	5
β-strand	29-32	4	5
β-strand	35	1	6
β-strand	54	1	6
α-helix	55-60	6
α-helix	62-64	3
β-strand	71-72	2	7
β-strand	75-76	2	7
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	5
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	5
α-helix	137-144	8
β-strand	150-155	6	8
β-strand	160-166	7	8
β-strand	169-170	2	8
α-helix	172-174	3
β-strand	176-178	3	8
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	9
β-strand	247-250	4	9
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	8
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	8
α-helix	333-337	5
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	5
α-helix	359-365	7
α-helix	367-370	4

Chain C: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	10
β-strand	16-21	6	10
β-strand	29-32	4	10
β-strand	35	1	11
β-strand	54	1	11
α-helix	55-58	4
β-strand	68	1	11
β-strand	71-72	2	12
β-strand	75-76	2	12
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	10
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	10
α-helix	137-144	8
β-strand	150-155	6	13
β-strand	160-166	7	13
β-strand	169-170	2	13
α-helix	172-174	3
β-strand	176-178	3	13
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	14
β-strand	247-250	4	14
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	287-294	8
β-strand	297-300	4	13
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	13
α-helix	333-337	5
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	10
α-helix	359-365	7
α-helix	367-370	4

Chain M: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	70-79	10
α-helix	84-89	6
α-helix	103-119	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C	protein	377	ORYCTOLAGUS CUNICULUS	P68135 (AlphaFold model)
Mkl/myocardin-like protein 1	M	protein	137	MUS MUSCULUS	Q8K4J6 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>2YJE_1 ACTIN, ALPHA SKELETAL MUSCLE (chains A, B, C)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (M), FASTA

>2YJE_2 MKL/MYOCARDIN-LIKE PROTEIN 1 (chains M)
GPGSLSERKNVLQLKLQQRRTREELVSQGIMPPLKSPAAFHEQRRSLERARTEDYLKRKI
RSRPERAELVRMHILEETSAEPSLQAKQLKLKRARLADDLNEKIAQRPGPMELVEKNILP
VESSLKEAIIVGQVNYP

Ligands and cofactors

ID	Name	Formula	Copies
LAB	Latrunculin B	C20 H29 N O5 S	3
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	3
MG	Magnesium ion	Mg	3

Primary citation

Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator. Mouilleron, S., Langer, C.A., Guettler, S. et al. Sci Signal (2011) 4:ra40-ra40. DOI 10.1126/scisignal.2001750 · 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

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