› 2bln

X-ray diffraction
1.2Å resolution

N-terminal formyltransferase domain of ArnA in complex with N-5- formyltetrahydrofolate and UMP

Released:
DOI: 10.2210/pdb2bln/pdb
PDB entry 2bln coloured by chain, front view.
PDB entry 2bln coloured by chain, side view.
PDB entry 2bln coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis.
Williams GJ, Breazeale SD, Raetz CR, Naismith JH
J Biol Chem 280 23000-8 (2005)
PMID: 15809294

Function and Biology Details

Reactions catalysed: 
UDP-alpha-D-glucuronate + NAD(+) = UDP-beta-L-threo-pentapyranos-4-ulose + CO(2) + NADH
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinose
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160160 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional polymyxin resistance protein ArnA Chains: A, B
Molecule details ›
Chains: A, B
Length: 305 amino acids
Theoretical weight: 33.25 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P77398 (Residues: 1-305; Coverage: 46%)
Gene names: JW2249, arnA, b2255, pmrI, yfbG
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FON 2 x FON
2 bound ligands:
Ligand U5P 2 x U5P
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 67.176Å b: 89.957Å c: 97.885Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.136 0.135 0.158
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Lipid A modification systems in gram-negative bacteria.
Raetz et al. (2007)
6 more

7 mentions without citation

The structural biology of enzymes involved in natural product glycosylation.
Singh et al. (2012)
6 more