› 5n9x

X-ray diffraction
2.4Å resolution

Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, ligand bound structure

Released:
DOI: 10.2210/pdb5n9x/pdb
PDB entry 5n9x coloured by chain, front view.
PDB entry 5n9x coloured by chain, side view.
PDB entry 5n9x coloured by chain, top view.
Source organism: Streptomyces sp.
Primary publication:
Structure of the adenylation domain Thr1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces sp. OH-5093-protein flexibility and molecular bases of substrate specificity.
Scaglione A, Fullone MR, Montemiglio LC, Parisi G, Zamparelli C, Vallone B, Savino C, Grgurina I
FEBS J 284 2981-2999 (2017)
PMID: 28704585

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124834 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylation domain Chains: A, B
Molecule details ›
Chains: A, B
Length: 529 amino acids
Theoretical weight: 57.72 KDa
Source organism: Streptomyces sp.
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: H6SG27 (Residues: 1-529; Coverage: 100%)
Gene name: thr1
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand THR 1 x THR
Ligand ATP 1 x ATP
Ligand MG 1 x MG
Ligand 8QN 1 x 8QN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2
Unit cell:
a: 179.022Å b: 52.524Å c: 110.119Å
α: 90° β: 105.95° γ: 90°
R-values:
R R work R free
0.203 0.199 0.276
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Structural basis of the nonribosomal codes for nonproteinogenic amino acid selective adenylation enzymes in the biosynthesis of natural products.
Kudo et al. (2019)
1 more

4 mentions without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)
3 more