› 5e8b

X-ray diffraction
1.62Å resolution

Crystal structure of the S. cerevisiae Rtf1 histone modification domain mutant R126A

Released:
DOI: 10.2210/pdb5e8b/pdb
Model geometry
Fit model/data
PDB entry 5e8b coloured by chain, front view.
PDB entry 5e8b coloured by chain, side view.
PDB entry 5e8b coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Directly Stimulates H2B Ubiquitylation through an Interaction with Rad6.
Van Oss SB, Shirra MK, Bataille AR, Wier AD, Yen K, Vinayachandran V, Byeon IL, Cucinotta CE, Héroux A, Jeon J, Kim J, VanDemark AP, Pugh BF, Arndt KM
Mol Cell 64 815-825 (2016)
PMID: 27840029

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156709 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA polymerase-associated protein RTF1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 67 amino acids
Theoretical weight: 8.15 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P53064 (Residues: 74-139; Coverage: 12%)
Gene names: CSL3, HRA458, RTF1, YGL244W

Ligands and Environments

2 bound ligands:
Ligand NA 3 x NA
Ligand BEN 1 x BEN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU FR-E DW
Spacegroup: R32
Unit cell:
a: 93.868Å b: 93.868Å c: 75.344Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.149 0.147 0.193
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Promoter-proximal pausing of RNA polymerase II: a nexus of gene regulation.
Core et al. (2019)
10 more

2 mentions without citation

The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Directly Stimulates H2B Ubiquitylation through an Interaction with Rad6.
Van Oss et al. (2016)
1 more