› 4ygx

X-ray diffraction
2.95Å resolution

Crystal Structure of D. melanogaster Ssu72+Symplekin bound to cis peptidomimetic CTD phospho-Ser5 peptide

Released:
DOI: 10.2210/pdb4ygx/pdb
PDB entry 4ygx coloured by chain, front view.
PDB entry 4ygx coloured by chain, side view.
PDB entry 4ygx coloured by chain, top view.
Source organisms:
Primary publication:
Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II.
Mayfield JE, Fan S, Wei S, Zhang M, Li B, Ellington AD, Etzkorn FA, Zhang YJ
ACS Chem Biol 10 2405-14 (2015)
PMID: 26332362

Function and Biology Details

Reaction catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero dimer
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-165374 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Symplekin Chains: A, C
Molecule details ›
Chains: A, C
Length: 339 amino acids
Theoretical weight: 37.5 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8MSU4 (Residues: 19-351; Coverage: 29%)
Gene names: CG2097, Sym
Sequence domains: Symplekin/PTA1 N-terminal
Structure domains: Leucine-rich Repeat Variant
RNA polymerase II subunit A C-terminal domain phosphatase SSU72 Chains: B, D
Molecule details ›
Chains: B, D
Length: 200 amino acids
Theoretical weight: 23.13 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9VWE4 (Residues: 1-195; Coverage: 100%)
Gene names: BEST:CK01830, CG14216, Dmel\CG14216, Dmel_CG14216, Ssu72, dSsu72
Sequence domains: Ssu72-like protein
Structure domains:
cis peptidomimetic CTD phospho-Ser5 peptide Chain: E
Molecule details ›
Chain: E
Length: 12 amino acids
Theoretical weight: 1.26 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P4
Unit cell:
a: 127.88Å b: 127.88Å c: 105.861Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.254
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

The isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target.
Zhou et al. (2016)
3 more

2 mentions without citation

Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II.
Mayfield et al. (2015)
1 more