› 5n82

X-ray diffraction
1.71Å resolution

Crystal structure of an engineered TycA variant in complex with an beta-Phe-AMP analog

Released:
DOI: 10.2210/pdb5n82/pdb
PDB entry 5n82 coloured by chain, front view.
PDB entry 5n82 coloured by chain, side view.
PDB entry 5n82 coloured by chain, top view.
Source organism: Brevibacillus parabrevis
Primary publication:
Nonribosomal biosynthesis of backbone-modified peptides.
Niquille DL, Hansen DA, Mori T, Fercher D, Kries H, Hilvert D
Nat Chem 10 282-287 (2018)
PMID: 29461527

Function and Biology Details

Reaction catalysed: 
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140551 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrocidine synthase 1 Chain: A
Molecule details ›
Chain: A
Length: 427 amino acids
Theoretical weight: 47.79 KDa
Source organism: Brevibacillus parabrevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P09095 (Residues: 3-418; Coverage: 38%)
Gene name: tycA
Sequence domains: AMP-binding enzyme
Structure domains: N-terminal domain of ligase-like

Ligands and Environments

3 bound ligands:
Ligand SO4 1 x SO4
Ligand BTB 1 x BTB
Ligand 8PZ 1 x 8PZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 59.611Å b: 60.368Å c: 123.778Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.171 0.2
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Directed Evolution of Protein Catalysts.
Zeymer et al. (2018)
13 more

1 mention without citation

Structure-guided function discovery of an NRPS-like glycine betaine reductase for choline biosynthesis in fungi.
Hai et al. (2019)