› 5o5o

X-ray diffraction
3.4Å resolution

X-ray crystal structure of RapZ from Escherichia coli (P32 space group)

Released:
DOI: 10.2210/pdb5o5o/pdb
PDB 5o5o coloured by chain and viewed from the front.
PDB 5o5o coloured by chain and viewed from the side.
PDB 5o5o coloured by chain and viewed from the top.
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. (2017)
PMID: 28977623

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (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: 284 amino acids
Theoretical weight: 32.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A894 (Residues: 1-284; Coverage: 100%)
Gene names: JW3172, b3205, rapZ, yhbJ
Sequence domains: P-loop ATPase protein family

Ligands and Environments

1 bound ligand:
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P32
Unit cell:
a: 92.75Å b: 92.75Å c: 156.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.197 0.266
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

RNA-binding proteins in bacteria.
Holmqvist et al. (2018)
4 other articles