› 5t9p

X-ray diffraction
2Å resolution

Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate

Released:
DOI: 10.2210/pdb5t9p/pdb
PDB entry 5t9p coloured by chain, front view.
PDB entry 5t9p coloured by chain, side view.
PDB entry 5t9p coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate.
Zhang J, Gonzalez LE, Hall TMT
OpenAccess logo Nucleic Acids Res 45 2829-2837 (2017)
PMID: 27789691

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-156902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosome biogenesis protein 15 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 111 amino acids
Theoretical weight: 13.05 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P53927 (Residues: 81-191; Coverage: 51%)
Gene names: N1954, NOP15, YNL110C
Sequence domains: RNA recognition motif

Ligands and Environments

2 bound ligands:
Ligand SO4 11 x SO4
Ligand CL 7 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 37.242Å b: 157.399Å c: 47.13Å
α: 90° β: 107.06° γ: 90°
R-values:
R R work R free
0.194 0.192 0.236
Expression system: Escherichia coli BL21

Quick links

Citations

7 citation in other articles

Intrinsically disordered electronegative clusters improve stability and binding specificity of RNA-binding proteins.
Zaharias et al. (2021)
6 more

1 mention without citation

Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate.
Zhang et al. (2017)