› 3sc6

X-ray diffraction
2.65Å resolution

2.65 Angstrom resolution crystal structure of dTDP-4-dehydrorhamnose reductase (rfbD) from Bacillus anthracis str. Ames in complex with NADP

Released:
DOI: 10.2210/pdb3sc6/pdb
PDB entry 3sc6 coloured by chain, front view.
PDB entry 3sc6 coloured by chain, side view.
PDB entry 3sc6 coloured by chain, top view.
Source organism: Bacillus anthracis str. Ames
Primary publication:
Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose reductase (RfbD).
Law A, Stergioulis A, Halavaty AS, Minasov G, Anderson WF, Kuhn ML
Acta Crystallogr F Struct Biol Commun 73 644-650 (2017)
PMID: 29199984

Function and Biology Details

Reaction catalysed: 
dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-105687 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dTDP-4-dehydrorhamnose reductase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 287 amino acids
Theoretical weight: 32.72 KDa
Source organism: Bacillus anthracis str. Ames
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A0A6L7H7R4 (Residues: 1-284; Coverage: 100%)
Gene names: GBAA_1231, rfbD
Sequence domains: RmlD substrate binding domain
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 6 x NAP
1 bound ligand:
Ligand SO4 17 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 79.449Å b: 113.337Å c: 144.949Å
α: 90° β: 91.18° γ: 90°
R-values:
R R work R free
0.217 0.215 0.258
Expression system: Escherichia coli BL21

Quick links

Citations

1 citations in other articles

The sps Genes Encode an Original Legionaminic Acid Pathway Required for Crust Assembly in Bacillus subtilis.
Dubois et al. (2020)

3 mentions without citation

GacA is essential for Group A Streptococcus and defines a new class of monomeric dTDP-4-dehydrorhamnose reductases (RmlD).
van der Beek et al. (2015)
2 more