› 6fdl

X-ray diffraction
1.75Å resolution

Crystal structure of the NYN domain of human MARF1

Released:
DOI: 10.2210/pdb6fdl/pdb
PDB entry 6fdl coloured by chain, front view.
PDB entry 6fdl coloured by chain, side view.
PDB entry 6fdl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human MARF1 is an endoribonuclease that interacts with the DCP1:2 decapping complex and degrades target mRNAs.
Nishimura T, Fakim H, Brandmann T, Youn JY, Gingras AC, Jinek M, Fabian MR
Nucleic Acids Res 46 12008-12021 (2018)
PMID: 30364987

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195239 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Meiosis regulator and mRNA stability factor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 160 amino acids
Theoretical weight: 18.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y4F3 (Residues: 352-500; Coverage: 9%)
Gene names: KIAA0430, LKAP, MARF1
Sequence domains: NYN domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P43212
Unit cell:
a: 96.867Å b: 96.867Å c: 63.096Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Diverse roles of biomolecular condensation in eukaryotic translational regulation.
Zhang et al. (2023)
12 other articles

1 mention without citation

Human MARF1 is an endoribonuclease that interacts with the DCP1:2 decapping complex and degrades target mRNAs.
Nishimura et al. (2018)