› 2d3d

X-ray diffraction
1.6Å resolution

crystal structure of the RNA binding SAM domain of saccharomyces cerevisiae Vts1

Released:
DOI: 10.2210/pdb2d3d/pdb
PDB entry 2d3d coloured by chain, front view.
PDB entry 2d3d coloured by chain, side view.
PDB entry 2d3d coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The NMR and X-ray structures of the Saccharomyces cerevisiae Vts1 SAM domain define a surface for the recognition of RNA hairpins.
Aviv T, Amborski AN, Zhao XS, Kwan JJ, Johnson PE, Sicheri F, Donaldson LW
J Mol Biol 356 274-9 (2006)
PMID: 16375924

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170697 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-binding protein VTS1 Chain: A
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 10.08 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q08831 (Residues: 436-523; Coverage: 17%)
Gene names: VTS1, YOR359W
Sequence domains: SAM domain (Sterile alpha motif)
Structure domains: Transcription Factor, Ets-1

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-002
Spacegroup: P212121
Unit cell:
a: 27.38Å b: 27.89Å c: 99.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.256
Expression system: Escherichia coli BL21

Quick links

Citations

13 citation in other articles

Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p.
Aviv et al. (2006)
12 more

4 mentions without citation

The complex of Sphingomonas elodea ATCC 31461 glucose-1-phosphate uridylyltransferase with glucose-1-phosphate reveals a novel quaternary structure, unique among nucleoside diphosphate-sugar pyrophosphorylase members.
Aragão et al. (2007)
3 more