1YAG: Yeast actin-human gelsolin segment 1 complex

Structure of the yeast actin-human gelsolin segment 1 complex. Determined by X-ray diffraction at 1.9 Å resolution. Released 9 Oct 1999.

Method: X-ray diffraction
Resolution: 1.9 Å
Organisms: Saccharomyces cerevisiae, Homo sapiens
Chains: 2
Atoms: 4,348
Mol. weight: 56.48 kDa
Ligands: MG, ATP, CA
Released: 9 Oct 1999

Explore 1YAG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1YAG contains 31 α-helices and 28 β-strands across 2 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: 25 helices, 21 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	22	1	2
β-strand	24	1	2
β-strand	29-32	4	1
β-strand	35-38	4	3
β-strand	53-54	2	3
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	3
β-strand	71-72	2	4
β-strand	75-76	2	4
α-helix	79-88	10
α-helix	89-94	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	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	182-194	13
α-helix	203-216	14
α-helix	223-228	6
β-strand	238-241	4	6
β-strand	247-250	4	6
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	5
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	5
α-helix	338-348	11
α-helix	350-354	5
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain G: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	6-10	5
β-strand	16-23	8	7
β-strand	26-29	4	7
α-helix	30-31	2
α-helix	32-34	3
β-strand	37-39	3	8
β-strand	43-51	9	7
β-strand	57-65	9	7
α-helix	71-87	17
β-strand	92-98	7	7
α-helix	104-107	4
β-strand	115-117	3	8
α-helix	122-123	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (ACTIN)	A	protein	375	Saccharomyces cerevisiae	P60010 (AlphaFold model)
Protein (gelsolin)	G	protein	125	Homo sapiens	P06396 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1YAG_1 PROTEIN (ACTIN) (chains A)
MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQS
KRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMT
QIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDL
AGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSY
ELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMS
GGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQ
EYDESGPSIVHHKCF

Sequence of entity 2 (G), FASTA

>1YAG_2 PROTEIN (GELSOLIN) (chains G)
MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYD
LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG
VASGF

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
CA	Calcium ion	Ca	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism. Vorobiev, S., Strokopytov, B., Drubin, D.G. et al. Proc Natl Acad Sci U S A (2003) 100:5760-5765. DOI 10.1073/pnas.0832273100 · PubMed

Other PDB entries of the same protein (UniProt P60010 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1YVN 2.1 Å, The yeast actin val 159 asn mutant complex with human gelsolin segment 1.
9GO5 2.5 Å, CryoEM Reconstruction of Yeast ADP-Actin Filament at 2.5 A resolution.
5NBL 2.8 Å, Crystal structure of the Arp4-N-actin(APO-state) heterodimer bound by a nanobody
7VVY 3.1 Å, TRA module of NuA4
8ESC 3.1 Å, Structure of the Yeast NuA4 Histone Acetyltransferase Complex
8A5O 3.2 Å, Structure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of S. cerevisiae INO80
8A5A 3.3 Å, Structure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of INO80
5NBM 3.4 Å, Crystal structure of the Arp4-N-actin(ATP-state) heterodimer bound by a nanobody
7YFN 3.8 Å, Core module of the NuA4 complex in S. cerevisiae
5NBN 4.0 Å, Crystal structure of the Arp4-N-actin-Arp8-Ino80HSA module of INO80
7YFP 4.0 Å, The NuA4 histone acetyltransferase complex from S. cerevisiae
5Y81 4.7 Å, NuA4 TEEAA sub-complex

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