› 5t8u

X-ray diffraction
2.32Å resolution

Crystal structure of P. falciparum LipL1 in complex lipoate

Released:
DOI: 10.2210/pdb5t8u/pdb
PDB entry 5t8u coloured by chain, front view.
PDB entry 5t8u coloured by chain, side view.
PDB entry 5t8u coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum.
Guerra AJ, Afanador GA, Prigge ST
Proteins 85 1777-1783 (2017)
PMID: 28543853

Function and Biology Details

Reaction catalysed: 
(1a) ATP + (R)-lipoate = lipoyl-AMP + diphosphate
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184755 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipoate--protein ligase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 360 amino acids
Theoretical weight: 42.2 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8IEG9 (Residues: 20-407; Coverage: 86%)
Gene names: LipL1, LplA, LplA1, PF3D7_1314600
Sequence domains:
Structure domains: Bira Bifunctional Protein; Domain 2

Ligands and Environments

1 bound ligand:
Ligand LPA 2 x LPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P3221
Unit cell:
a: 120.24Å b: 120.24Å c: 134.92Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.274 0.273 0.302
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Understanding and Engineering Glycine Cleavage System and Related Metabolic Pathways for C1-Based Biosynthesis.
Ren et al. (2022)
1 other article

3 mentions without citation

Lipoic Acid Metabolism as a Potential Chemotherapeutic Target Against Plasmodium falciparum and Staphylococcus aureus.
Rei Yan et al. (2021)
2 more