› 6bwl

X-ray diffraction
1.45Å resolution

X-ray structure of Pal from Bacillus thuringiensis

Released:
DOI: 10.2210/pdb6bwl/pdb
PDB entry 6bwl coloured by chain, front view.
PDB entry 6bwl coloured by chain, side view.
PDB entry 6bwl coloured by chain, top view.
Source organism: Bacillus thuringiensis serovar israelensis ATCC 35646
Primary publication:
Molecular architectures of Pen and Pal: Key enzymes required for CMP-pseudaminic acid biosynthesis in Bacillus thuringiensis.
Delvaux NA, Thoden JB, Holden HM
Protein Sci 27 738-749 (2018)
PMID: 29266550

Function and Biology Details

Reaction catalysed: 
dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174528 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent epimerase/dehydratase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 328 amino acids
Theoretical weight: 36.74 KDa
Source organism: Bacillus thuringiensis serovar israelensis ATCC 35646
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3ESA4 (Residues: 1-320; Coverage: 100%)
Gene name: RBTH_04254
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
4 bound ligands:
Ligand UDP 1 x UDP
Ligand EDO 4 x EDO
Ligand CL 2 x CL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2221
Unit cell:
a: 96.42Å b: 98.341Å c: 98.603Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.131 0.129 0.151
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Type III Secretion Effectors with Arginine N-Glycosyltransferase Activity.
Araujo-Garrido et al. (2020)
1 more

1 mention without citation

Molecular architectures of Pen and Pal: Key enzymes required for CMP-pseudaminic acid biosynthesis in Bacillus thuringiensis.
Delvaux et al. (2018)