5V3N: S. cerevisiae Ulp2-Tof2-Csm1 complex

Structure of S. cerevisiae Ulp2-Tof2-Csm1 complex. Determined by X-ray diffraction at 1.3 Å resolution. Released 17 May 2017.

Method: X-ray diffraction
Resolution: 1.3 Å
Organisms: Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Saccharomyces cerevisiae x Saccharomyces kudriavzevii, Saccharomyces cerevisiae
Chains: 2
Atoms: 1,240
Mol. weight: 17.26 kDa
Released: 17 May 2017

Explore 5V3N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5V3N contains 9 α-helices and 6 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: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	71-82	12
β-strand	84-91	8	1
β-strand	95-104	10	1
β-strand	114-124	11	1
α-helix	126-128	3
β-strand	130-136	7	1
α-helix	143-152	10
α-helix	155-158	4
β-strand	161-164	4	1
α-helix	165-167	3
α-helix	168-179	12

Chain B: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	26-29	4
α-helix	31-32	2
α-helix	34-38	5
β-strand	54-55	2	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Monopolin complex subunit CSM1	A	protein	113	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P25651 (AlphaFold model)
Ulp2p,Topoisomerase 1-associated factor 2 chimera	B	protein	38	Saccharomyces cerevisiae x Saccharomyces kudriavzevii, Saccharomyces cerevisiae	H0GHZ9, Q02208 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5V3N_1 Monopolin complex subunit CSM1 (chains A)
ENSEVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGGSSDDYSIMDYKLGFVKGQAQ
VTEVIYAPVLKQRSTEELYSLQSKLPEYLFETLSFPLSSLNQFYNKIAKSLNK

Sequence of entity 2 (B), FASTA

>5V3N_2 Ulp2p,Topoisomerase 1-associated factor 2 chimera (chains B)
SNAPYFGRPSLKTRAKQFEGVSSKDIGENCRRIEAFSD

Primary citation

Recruitment of a SUMO isopeptidase to rDNA stabilizes silencing complexes by opposing SUMO targeted ubiquitin ligase activity. Liang, J., Singh, N., Carlson, C.R. et al. Genes Dev (2017) 31:802-815. DOI 10.1101/gad.296145.117 · PubMed

Other PDB entries of the same protein (UniProt P25651 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6DEI 1.7 Å, Structure of Dse3-Csm1 complex
5V1A 2.14 Å, Structure of S. cerevisiae Ulp2:Csm1 complex
3N4S 2.35 Å, Structure of Csm1 C-terminal domain, P21212 form
3N4R 2.6 Å, Structure of Csm1 C-terminal domain, R3 form
5KTB 3.05 Å, Structure of a complex between S. cerevisiae Csm1 and Mam1
3N4X 3.41 Å, Structure of Csm1 full-length
3N7N 3.9 Å, Structure of Csm1/Lrs4 complex

Browse structure collections

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