› 1eo0

Solution NMR

CONSERVED DOMAIN COMMON TO TRANSCRIPTION FACTORS TFIIS, ELONGIN A, CRSP70

Released:
DOI: 10.2210/pdb1eo0/pdb
PDB entry 1eo0 coloured by chain, ensemble of 10 models, front view.
PDB entry 1eo0 coloured by chain, ensemble of 10 models, side view.
PDB entry 1eo0 coloured by chain, ensemble of 10 models, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70.
Booth V, Koth CM, Edwards AM, Arrowsmith CH
J Biol Chem 275 31266-8 (2000)
PMID: 10811649

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139469 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription elongation factor S-II Chain: A
Molecule details ›
Chain: A
Length: 77 amino acids
Theoretical weight: 8.82 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Bacteria
UniProt:
  • Canonical: P07273 (Residues: 1-77; Coverage: 25%)
Gene names: DST1, PPR2, YGL043W
Sequence domains: TFIIS helical bundle-like domain
Structure domains: Conserved domain common to transcription factors TFIIS, elongin A, CRSP70

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing molecular dynamics
Expression system: Bacteria

Quick links

Citations

6 review citations

Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution.
Ceulemans et al. (2002)
5 more

7 mentions without citation

The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition.
Kamtekar et al. (2006)
6 more