› 6vl1

X-ray diffraction
2.1Å resolution

Crystal Structure of the N-prenyltransferase DabA in Complex with NGG and Mg2+

Released:
DOI: 10.2210/pdb6vl1/pdb
PDB entry 6vl1 coloured by chain, front view.
PDB entry 6vl1 coloured by chain, side view.
PDB entry 6vl1 coloured by chain, top view.
Source organism: Pseudo-nitzschia multiseries
Primary publication:
Algal neurotoxin biosynthesis repurposes the terpene cyclase structural fold into an N-prenyltransferase.
Chekan JR, McKinnie SMK, Noel JP, Moore BS
Proc Natl Acad Sci U S A 117 12799-12805 (2020)
PMID: 32457155

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-104766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Magnesium-dependent glutamate N-prenyltransferase Chain: A
Molecule details ›
Chain: A
Length: 441 amino acids
Theoretical weight: 51.57 KDa
Source organism: Pseudo-nitzschia multiseries
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A386KZ50 (Residues: 46-482; Coverage: 91%)
Gene name: dabA
Sequence domains: Terpene synthase family 2, C-terminal metal binding

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand R1V 1 x R1V
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P43212
Unit cell:
a: 123.425Å b: 123.425Å c: 113.208Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.176 0.195
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Recent trends in biocatalysis.
Yi et al. (2021)
3 more

1 mention without citation

Algal neurotoxin biosynthesis repurposes the terpene cyclase structural fold into an N-prenyltransferase.
Chekan et al. (2020)