› 5cqs

X-ray diffraction
2.7Å resolution

Dimerization of Elp1 is essential for Elongator complex assembly

Released:
DOI: 10.2210/pdb5cqs/pdb
PDB entry 5cqs coloured by chain, front view.
PDB entry 5cqs coloured by chain, side view.
PDB entry 5cqs coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Dimerization of elongator protein 1 is essential for Elongator complex assembly.
Xu H, Lin Z, Li F, Diao W, Dong C, Zhou H, Xie X, Wang Z, Shen Y, Long J
Proc Natl Acad Sci U S A 112 10697-702 (2015)
PMID: 26261306

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170382 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Elongator complex protein 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 435 amino acids
Theoretical weight: 50.23 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q06706 (Residues: 919-1349; Coverage: 32%)
Gene names: ELP1, IKI3, L3502.7, TOT1, YLR384C

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: C2
Unit cell:
a: 127.754Å b: 157.744Å c: 139.264Å
α: 90° β: 93.09° γ: 90°
R-values:
R R work R free
0.236 0.234 0.256
Expression system: Escherichia coli

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Citations

8 review citations

Familial dysautonomia: History, genotype, phenotype and translational research.
Norcliffe-Kaufmann et al. (2017)
7 more

6 mentions without citation

Resonance Raman view of the active site architecture in bacterial DyP-type peroxidases.
Silveira et al. (2020)
5 more