› 1wki

Solution NMR

solution structure of ribosomal protein L16 from thermus thermophilus HB8

Released:
DOI: 10.2210/pdb1wki/pdb
PDB entry 1wki coloured by chain, ensemble of 30 models, front view.
PDB entry 1wki coloured by chain, ensemble of 30 models, side view.
PDB entry 1wki coloured by chain, ensemble of 30 models, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Solution structure of ribosomal protein L16 from Thermus thermophilus HB8.
Nishimura M, Yoshida T, Shirouzu M, Terada T, Kuramitsu S, Yokoyama S, Ohkubo T, Kobayashi Y
J Mol Biol 344 1369-83 (2004)
PMID: 15561149

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158022 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Large ribosomal subunit protein uL16 Chain: A
Molecule details ›
Chain: A
Length: 141 amino acids
Theoretical weight: 15.99 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P60489 (Residues: 1-141; Coverage: 100%)
Gene names: TTHA1685, rplP
Sequence domains: Ribosomal protein L16p/L10e
Structure domains: Ribosomal protein L10e/L16

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

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Citations

6 review citations

Ribosomal proteins in the spotlight.
Wilson et al. (2005)
5 more

1 mention without citation

Post-translational hydroxylation by 2OG/Fe(II)-dependent oxygenases as a novel regulatory mechanism in bacteria.
van Staalduinen et al. (2014)