› 2l2n

Solution NMR

Backbone 1H, 13C, and 15N Chemical Shift Assignments for the first dsRBD of protein HYL1

Released:
DOI: 10.2210/pdb2l2n/pdb
PDB entry 2l2n coloured by chain, ensemble of 10 models, front view.
PDB entry 2l2n coloured by chain, ensemble of 10 models, side view.
PDB entry 2l2n coloured by chain, ensemble of 10 models, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structure and RNA interactions of the plant MicroRNA processing-associated protein HYL1.
Rasia RM, Mateos J, Bologna NG, Burdisso P, Imbert L, Palatnik JF, Boisbouvier J
Biochemistry 49 8237-9 (2010)
PMID: 20735118

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126446 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Double-stranded RNA-binding protein 1 Chain: A
Molecule details ›
Chain: A
Length: 103 amino acids
Theoretical weight: 11.39 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: O04492 (Residues: 1-100; Coverage: 24%)
Gene names: At1g09700, DRB1, F21M12.9, HYL1
Sequence domains: Double-stranded RNA binding motif
Structure domains: Double Stranded RNA Binding Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 41%
Refinement method: rosetta full atom relaxation
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Biogenesis, turnover, and mode of action of plant microRNAs.
Rogers et al. (2013)
5 more

2 mentions without citation

RNA recognition by double-stranded RNA binding domains: a matter of shape and sequence.
Masliah et al. (2013)
1 more