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› 5o5q

X-ray diffraction
3.25Å resolution

X-ray crystal structure of RapZ from Escherichia coli (P3221 space group)

Released:
DOI: 10.2210/pdb5o5q/pdb
Model geometry
Fit model/data
PDB entry 5o5q coloured by chain, front view.
PDB entry 5o5q coloured by chain, side view.
PDB entry 5o5q coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural insights into RapZ-mediated regulation of bacterial amino-sugar metabolism.
Gonzalez GM, Durica-Mitic S, Hardwick SW, Moncrieffe MC, Resch M, Neumann P, Ficner R, Görke B, Luisi BF
OpenAccess logo Nucleic Acids Res 45 10845-10860 (2017)
PMID: 28977623

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141685 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNase adapter protein RapZ Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 295 amino acids
Theoretical weight: 33.87 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A894 (Residues: 1-284; Coverage: 100%)
Gene names: JW3172, b3205, rapZ, yhbJ
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 15 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P3221
Unit cell:
a: 91.54Å b: 91.54Å c: 352.55Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.218 0.273
Expression system: Escherichia coli

Quick links

Citations

6 review citations

RNA-binding proteins in bacteria.
Holmqvist et al. (2018)
5 more

3 mentions without citation

Structural insights into RapZ-mediated regulation of bacterial amino-sugar metabolism.
Gonzalez et al. (2017)
2 more