› 4m38

X-ray diffraction
2.2Å resolution

Crystal structure of Trypanosoma brucei protein arginine methyltransferase 7 complex with AdoHcy and histone H4 peptide

Released:
DOI: 10.2210/pdb4m38/pdb
PDB entry 4m38 coloured by chain, front view.
PDB entry 4m38 coloured by chain, side view.
PDB entry 4m38 coloured by chain, top view.
Source organisms:
Primary publication:
Structural determinants for the strict monomethylation activity by trypanosoma brucei protein arginine methyltransferase 7.
Wang C, Zhu Y, Caceres TB, Liu L, Peng J, Wang J, Chen J, Chen X, Zhang Z, Zuo X, Gong Q, Teng M, Hevel JM, Wu J, Shi Y
Structure 22 756-68 (2014)
PMID: 24726341

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158696 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein arginine N-methyltransferase 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 343 amino acids
Theoretical weight: 38.99 KDa
Source organism: Trypanosoma brucei brucei TREU927
Expression system: Escherichia coli
UniProt:
  • Canonical: Q582G4 (Residues: 36-378; Coverage: 88%)
Gene names: PRMT7, Tb927.7.5490
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:
Histone H4 Chains: E, F
Molecule details ›
Chains: E, F
Length: 21 amino acids
Theoretical weight: 2.1 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P62805 (Residues: 2-22; Coverage: 20%)
Gene names: H4-16, H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4C1, H4C11, H4C12, H4C13, H4C14, H4C15, H4C16, H4C2, H4C3, H4C4, H4C5, H4C6, H4C8, H4C9, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4

Ligands and Environments

1 bound ligand:
Ligand SAH 2 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 66.696Å b: 72.764Å c: 72.565Å
α: 90° β: 110.94° γ: 90°
R-values:
R R work R free
0.19 0.188 0.23
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

Biochemistry and regulation of the protein arginine methyltransferases (PRMTs).
Morales et al. (2016)
1 more

12 mentions without citation

Chemical biology of protein arginine modifications in epigenetic regulation.
Fuhrmann et al. (2015)
11 more