4PL8: Rabbit skeletal muscle actin

Structure of rabbit skeletal muscle actin in complex with a hybrid peptide comprising thymosin beta4 and the lysine-rich region of Cordon-Bleu. Determined by X-ray diffraction at 2.0 Å resolution. Released 22 Oct 2014.

Method: X-ray diffraction
Resolution: 2.0 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 3
Atoms: 6,298
Mol. weight: 93.18 kDa
Ligands: CA, ATP
Released: 22 Oct 2014

Explore 4PL8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PL8 contains 54 α-helices and 41 β-strands across 3 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: 26 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	24	1	2
β-strand	29-32	4	1
β-strand	35-37	3	3
β-strand	53-54	2	3
α-helix	56-59	4
β-strand	66-68	3	3
β-strand	71-72	2	4
β-strand	75-76	2	4
α-helix	79-87	9
α-helix	88-94	7
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	5
β-strand	160-166	7	5
β-strand	169-170	2	5
α-helix	172-174	3
β-strand	176-178	3	5
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	6
β-strand	247-250	4	6
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	5
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	5
α-helix	335-337	3
α-helix	338-346	9
α-helix	350-355	6
α-helix	356	1
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain B: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	7
β-strand	16-21	6	7
β-strand	29-32	4	7
β-strand	35-36	2	8
β-strand	53-54	2	8
α-helix	55-57	3
β-strand	67-68	2	8
β-strand	71-72	2	9
β-strand	75-76	2	9
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	7
α-helix	113-125	13
β-strand	131-136	6	7
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	182-195	14
α-helix	206-216	11
α-helix	223-229	7
α-helix	230-232	3
β-strand	238-241	4	11
β-strand	247-250	4	11
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	10
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	10
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
α-helix	356	1
β-strand	357-358	2	7
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain H: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	35-40	6
α-helix	44-46	3
β-strand	48	1	2
α-helix	49	1
α-helix	51-52	2
β-strand	53	1	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B	protein	375	Oryctolagus cuniculus	P68135 (AlphaFold model)
Thymosin beta-4,Protein cordon-bleu,Thymosin beta-4	H	protein	73	Homo sapiens	O75128 (AlphaFold model), P62328 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4PL8_1 Actin, alpha skeletal muscle (chains A, B)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF

Sequence of entity 2 (H), FASTA

>4PL8_2 Thymosin beta-4,Protein cordon-bleu,Thymosin beta-4 (chains H)
GPSDKPDMAEIEKFDKSKFKPVVQRPVPKDSDKPDMAEIEKFDKSKLKKTETQEKNPLPS
KETIEQEKQAGES

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2

Primary citation

Structural basis of thymosin-beta 4/profilin exchange leading to actin filament polymerization. Xue, B., Leyrat, C., Grimes, J.M. et al. Proc Natl Acad Sci U S A (2014) 111:E4596-E4605. DOI 10.1073/pnas.1412271111 · 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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