› 3tr9

X-ray diffraction
1.9Å resolution

Structure of a dihydropteroate synthase (folP) in complex with pteroic acid from Coxiella burnetii

Released:
DOI: 10.2210/pdb3tr9/pdb
PDB entry 3tr9 coloured by chain, front view.
PDB entry 3tr9 coloured by chain, side view.
PDB entry 3tr9 coloured by chain, top view.
Source organism: Coxiella burnetii
Primary publication:
Structural genomics for drug design against the pathogen Coxiella burnetii.
Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD
Proteins 83 2124-36 (2015)
PMID: 26033498

Function and Biology Details

Reaction catalysed: 
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182913 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dihydropteroate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 314 amino acids
Theoretical weight: 35.88 KDa
Source organism: Coxiella burnetii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83BY6 (Residues: 1-297; Coverage: 100%)
Gene names: CBU_1351, folP
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

3 bound ligands:
Ligand PT1 4 x PT1
Ligand CL 2 x CL
Ligand NA 3 x NA
1 modified residue:
Ligand MSE 36 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 86.877Å b: 86.883Å c: 158.159Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.212
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.
Martins et al. (2015)
4 more

1 mention without citation

Molecular mechanism of plasmid-borne resistance to sulfonamide antibiotics.
Venkatesan et al. (2023)