6DEI: Dse3-Csm1 complex

Structure of Dse3-Csm1 complex. Determined by X-ray diffraction at 1.7 Å resolution. Released 3 Oct 2018.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 4
Atoms: 2,318
Mol. weight: 31.75 kDa
Released: 3 Oct 2018

Explore 6DEI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6DEI contains 14 α-helices and 12 β-strands across 4 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	95-105	11	1
β-strand	113-124	12	1
β-strand	130-136	7	1
α-helix	138-140	3
α-helix	143-152	10
α-helix	155-158	4
β-strand	161-163	3	1
α-helix	165-167	3
α-helix	168-180	13

Chain B: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	72-82	11
β-strand	84-91	8	2
β-strand	96-103	8	2
α-helix	104-106	3
β-strand	115-122	8	2
β-strand	131-136	6	2
α-helix	143-152	10
α-helix	155-158	4
β-strand	161-164	4	2
α-helix	165-167	3
α-helix	168-179	12

Chain C: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	59	1	3
β-strand	62	1	3
α-helix	65-67	3

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	65-72	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Monopolin complex subunit CSM1	A, B	protein	113	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P25651 (AlphaFold model)
Protein DSE3	C, D	protein	24	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	Q08729 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6DEI_1 Monopolin complex subunit CSM1 (chains A, B)
ENSEVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGGSSDDYSIMDYKLGFVKGQAQ
VTEVIYAPVLKQRSTEELYSLQSKLPEYLFETLSFPLSSLNQFYNKIAKSLNK

Sequence of entity 2 (C, D), FASTA

>6DEI_2 Protein DSE3 (chains C, D)
SNAFGGTLKLKKRLESVPELFLHD

Primary citation

The budding-yeast RWD protein Csm1 scaffolds diverse protein complexes through a conserved structural mechanism. Singh, N., Corbett, K.D. Protein Sci (2018) 27:2094-2100. DOI 10.1002/pro.3515 · PubMed

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

5V3N 1.3 Å, Structure of S. cerevisiae Ulp2-Tof2-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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