4DT1: Psy3-Csm2 complex

Crystal structure of the Psy3-Csm2 complex. Determined by X-ray diffraction at 1.9 Å resolution. Released 11 Apr 2012.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 3,293
Mol. weight: 53.73 kDa
Ligands: EOH
Released: 11 Apr 2012

Explore 4DT1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4DT1 contains 24 α-helices and 13 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: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
β-strand	9-13	5	1
α-helix	17-28	12
β-strand	34-41	8	1
α-helix	48-54	7
α-helix	60-62	3
α-helix	63-67	5
β-strand	69-73	5	1
α-helix	77-97	21
β-strand	110-117	8	1
α-helix	119-129	11
α-helix	132-151	20
β-strand	157-165	9	1
α-helix	167-170	4
α-helix	171-175	5
α-helix	199-206	8
β-strand	210-211	2	1

Chain B: 13 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	12-14	3
α-helix	27-29	3
α-helix	35-38	4
β-strand	43-48	6	2
α-helix	53-54	2
α-helix	55-60	6
β-strand	68-74	7	2
β-strand	89-92	4	2
α-helix	95-97	3
α-helix	100-112	13
α-helix	114-119	6
β-strand	129-136	8	2
α-helix	138-141	4
α-helix	152-171	20
β-strand	174-179	6	2
α-helix	182-185	4
α-helix	188-190	3
α-helix	213-216	4
β-strand	221-226	6	2
β-strand	233-236	4	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chromosome segregation in meiosis protein 2	A	protein	213	Saccharomyces cerevisiae	P40465 (AlphaFold model)
Platinum sensitivity protein 3	B	protein	245	Saccharomyces cerevisiae	Q12318 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4DT1_1 Chromosome segregation in meiosis protein 2 (chains A)
MEYEDLELITIWPSPTKNKLCQFIKQNLSKEHVVTQLFFIDATSSFPLSQFQKLVPPTLP
ENVRIYENIRINTCLDLEELSAITVKLLQILSMNKINAQRGTEDAVTEPLKIILYINGLE
VMFRNSQFKSSPQRSHELLRDTLLKLRVMGNDENENASIRTLLEFPKEQLLDYYLKKNNN
TRTSSVRSKRRRIKNGDSLAEYIWKYYADSLFE

Sequence of entity 2 (B), FASTA

>4DT1_2 Platinum sensitivity protein 3 (chains B)
GSHMEVLKNIRIYPLSNFITSTKNYINLPNELRNLISEEQESKLGFLHIIESDFKPSVAL
QKLVNCTTGDEKILIIDIVSIWSQQKQRQHGAIYMNSLSCINITGLIVFLELLYDSPMDA
LRRCQVDNFNFQLRGIVIDNLSFLNFESDKNYDVINLSKFEKLFKILRKLREFLGCWIIT
KSFPTDFYNGIENTLVDKWSIKRKSGVTLYPTKLPDSYMKGMDLIIYREVVDGRPQYRRI
AALEE

Ligands and cofactors

ID	Name	Formula	Copies
EOH	Ethanol	C2 H6 O	4

Primary citation

Structural analysis of Shu proteins reveals a DNA binding role essential for resisting damage. Tao, Y., Li, X., Liu, Y. et al. J Biol Chem (2012) 287:20231-20239. DOI 10.1074/jbc.M111.334698 · PubMed

Other PDB entries of the same protein (UniProt P40465 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3VU9 1.75 Å, Crystal Structure of Psy3-Csm2 complex
4EQ6 1.8 Å, The crystal structure of Psy3-Csm2 complex from budding yeast
9Q2H 2.74 Å, Rad55-Rad57-SHU homologous recombination complex
9Q2I 3.0 Å, Rad55-Rad57-SHU homologous recombination complex
9Q2C 3.06 Å, Rad55-Rad57-SHU-Rad51 bound to ssDNA with AMP-PNP
9Q2F 3.06 Å, Rad55-Rad57-SHU-Rad51-Rad51 bound to ssDNA with AMP-PNP
5XYN 3.3 Å, The crystal structure of Csm2-Psy3-Shu1-Shu2 complex from budding yeast
9Q2E 3.44 Å, Rad55-Rad57-SHU bound to ssDNA
9Q2L 3.7 Å, Rad55-Rad57(E161Q)-SHU-3xRad51 bound to ssDNA with ATP

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