3ced

X-ray diffraction
2.15Å resolution

Crystal structure of the C-terminal NIL domain of an ABC transporter protein homologue from Staphylococcus aureus

Released:
Entry authors: Cuff ME, Bigelow L, Clancy S, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
ATP + H(2)O + D-methionine-[methionine-binding protein](Side 1) = ADP + phosphate + D-methionine(Side 2) + [methionine-binding protein](Side 1)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-189402 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine import ATP-binding protein MetN 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 98 amino acids
Theoretical weight: 11.02 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99VG8 (Residues: 247-341; Coverage: 28%)
Gene names: SAV0837, metN2
Sequence domains: NIL domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I422
Unit cell:
a: 132.55Å b: 132.55Å c: 132.083Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.215
Expression system: Escherichia coli BL21(DE3)