3r07

X-ray diffraction
2.7Å resolution

Structural analysis of an archaeal lipoylation system. A bi-partite lipoate protein ligase and its E2 lipoyl domain from Thermoplasma acidophilum

Released:
Entry authors: Posner MG, Upadhyay U, Crennell S

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-190880 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lipoate-protein ligase A subunit 1 Chain: A
Molecule details ›
Chain: A
Length: 285 amino acids
Theoretical weight: 32.7 KDa
Source organism: Thermoplasma acidophilum DSM 1728
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HKT1 (Residues: 1-262; Coverage: 100%)
Gene names: Ta0514, lplA
Sequence domains: Biotin/lipoate A/B protein ligase family
Structure domains: Bira Bifunctional Protein; Domain 2
Lipoate-protein ligase A subunit 2 Chain: C
Molecule details ›
Chain: C
Length: 91 amino acids
Theoretical weight: 10.56 KDa
Source organism: Thermoplasma acidophilum DSM 1728
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HKT2 (Residues: 7-94; Coverage: 94%)
Gene names: Ta0513, lplB
Sequence domains: Bacterial lipoate protein ligase C-terminus
Structure domains: CO dehydrogenase flavoprotein, C-terminal domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P3121
Unit cell:
a: 118.57Å b: 118.57Å c: 72.92Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.254
Expression system: Escherichia coli