2V51: MAL-RPEL1 complexed to actin

Structure of MAL-RPEL1 complexed to actin. Determined by X-ray diffraction at 2.35 Å resolution. Released 25 Nov 2008.

Method: X-ray diffraction
Resolution: 2.35 Å
Organisms: ORYCTOLAGUS CUNICULUS, MUS MUSCULUS
Chains: 4
Atoms: 6,235
Mol. weight: 94.09 kDa
Ligands: ATP, CA, LAB, SCN
Released: 25 Nov 2008

Explore 2V51 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2V51 contains 54 α-helices and 40 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 B: 24 helices, 19 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	35-36	2	2
β-strand	53-54	2	2
α-helix	56-59	4
β-strand	67-68	2	2
β-strand	71-72	2	3
β-strand	75-76	2	3
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	4
β-strand	160-166	7	4
β-strand	169-170	2	4
α-helix	172-174	3
β-strand	176-178	3	4
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-259	7
α-helix	264-267	4
α-helix	271-273	3
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	4
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-370	4

Chain D: 23 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	6
β-strand	16-21	6	6
β-strand	22	1	7
β-strand	24	1	7
β-strand	29-32	4	6
β-strand	35-37	3	8
β-strand	53-54	2	8
α-helix	56-59	4
β-strand	66-68	3	8
β-strand	71-72	2	9
β-strand	75-76	2	9
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	6
α-helix	113-125	13
β-strand	131-136	6	6
α-helix	137-144	8
β-strand	150-155	6	10
β-strand	160-166	7	10
β-strand	169-170	2	10
α-helix	172-174	3
β-strand	176-178	3	10
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	11
β-strand	247-250	4	11
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	10
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	10
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	6
α-helix	359-363	5
α-helix	367-370	4

Chain E: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	72-80	9
α-helix	81-83	3
α-helix	84-89	6

Chain F: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	72-79	8
α-helix	81-83	3
α-helix	84-90	7
α-helix	94-96	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	B, D	protein	377	ORYCTOLAGUS CUNICULUS	P68135 (AlphaFold model)
Mkl/myocardin-like protein 1	E, F	protein	32	MUS MUSCULUS	Q8K4J6 (AlphaFold model)

Sequence of entity 1 (B, D), FASTA

>2V51_1 ACTIN, ALPHA SKELETAL MUSCLE (chains B, D)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (E, F), FASTA

>2V51_2 MKL/MYOCARDIN-LIKE PROTEIN 1 (chains E, F)
LSERKNVLQLKLQQRRTREELVSQGIMPPLKS

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
CA	Calcium ion	Ca	2
LAB	Latrunculin B	C20 H29 N O5 S	2
SCN	Thiocyanate ion	C N S	4

Water and common crystallization additives (PEG) are not listed.

Primary citation

Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. Mouilleron, S., Guettler, S., Langer, C.A. et al. EMBO J (2008) 27:3198-3208. DOI 10.1038/emboj.2008.235 · 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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