8V2Z: Smooth Muscle Gamma Actin (ACTG2) Mutant R257C

Cryo-EM Structure of Smooth Muscle Gamma Actin (ACTG2) Mutant R257C. Determined by electron microscopy at 2.72 Å resolution. Released 1 May 2024.

Method: Electron microscopy
Resolution: 2.72 Å
Organism: Homo sapiens
Chains: 5
Atoms: 14,635
Mol. weight: 211.67 kDa
Ligands: ADP, MG
Released: 1 May 2024

Explore 8V2Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8V2Z contains 115 α-helices and 98 β-strands across 5 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, 19 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	29-32	4	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	137-145	9
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	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	4
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-347	10
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	370-373	4

Chain B: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-12	5	6
β-strand	16-21	6	6
β-strand	29-32	4	6
β-strand	35-38	4	7
β-strand	53-54	2	7
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	7
β-strand	71-72	2	8
β-strand	75-76	2	8
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	6
α-helix	113-125	13
β-strand	131-136	6	6
α-helix	137-145	9
β-strand	150-155	6	9
β-strand	160-166	7	9
β-strand	169-170	2	9
α-helix	172-174	3
β-strand	176-178	3	9
α-helix	182-192	11
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	10
β-strand	247-250	4	10
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	9
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	9
α-helix	338-347	10
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	370-373	4

Chain C: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-12	5	11
β-strand	16-21	6	11
β-strand	29-32	4	11
β-strand	35-38	4	12
β-strand	41-42	2	4
β-strand	53-54	2	12
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	12
β-strand	71-72	2	13
β-strand	75-76	2	13
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	11
α-helix	113-125	13
β-strand	131-136	6	11
α-helix	137-145	9
β-strand	150-155	6	14
β-strand	160-166	7	14
β-strand	169-170	2	14
α-helix	172-174	3
β-strand	176-178	3	14
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	15
β-strand	247-250	4	15
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	14
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	14
α-helix	338-347	10
β-strand	357-358	2	11
α-helix	359-365	7
α-helix	370-373	4

Chains D and E: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-12	5	16
β-strand	16-21	6	16
β-strand	29-32	4	16
β-strand	35-38	4	17
β-strand	41-42	2	9
β-strand	53-54	2	17
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	17
β-strand	71-72	2	18
β-strand	75-76	2	18
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	16
α-helix	113-125	13
β-strand	131-136	6	16
α-helix	137-145	9
β-strand	150-155	6	19
β-strand	160-166	7	19
β-strand	169-170	2	19
α-helix	172-174	3
β-strand	176-178	3	19
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	20
β-strand	247-250	4	20
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	19
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	338-347	10
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	370-373	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, gamma-enteric smooth muscle	A, B, C, D, E	protein	376	Homo sapiens	P63267 (AlphaFold model)

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

>8V2Z_1 Actin, gamma-enteric smooth muscle (chains A, B, C, D, E)
MCEEETTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD
LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS
YELPDGQVITIGNERFCCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVL
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISK
PEYDEAGPSIVHRKCF

Ligands and cofactors

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

Primary citation

Molecular mechanisms linking missense ACTG2 mutations to visceral myopathy. Ceron, R.H., Baez-Cruz, F.A., Palmer, N.J. et al. Sci Adv (2024) 10:eadn6615-eadn6615. DOI 10.1126/sciadv.adn6615 · PubMed

Other PDB entries of the same protein (UniProt P63267 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8V2O 2.45 Å, Cryo-EM Structure of Wildtype Smooth Muscle Gamma Actin (ACTG2)
8V30 2.54 Å, Smooth Muscle Gamma Actin (ACTG2) Filament Mutant R40C
6JAT 2.71 Å, Crystal structure of SETD3 bound to Actin peptide and SFG

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