› 5ey9

X-ray diffraction
2.5Å resolution

Structure of FadD32 from Mycobacterium marinum complexed to AMPC12

Released:
DOI: 10.2210/pdb5ey9/pdb
Model geometry
Fit model/data
PDB entry 5ey9 coloured by chain, front view.
PDB entry 5ey9 coloured by chain, side view.
PDB entry 5ey9 coloured by chain, top view.
Source organism: Mycobacterium marinum
Primary publication:
Insight into Structure-Function Relationships and Inhibition of the Fatty Acyl-AMP Ligase (FadD32) Orthologs from Mycobacteria.
Guillet V, Galandrin S, Maveyraud L, Ladevèze S, Mariaule V, Bon C, Eynard N, Daffé M, Marrakchi H, Mourey L
J Biol Chem 291 7973-89 (2016)
PMID: 26900152

Function and Biology Details

Reaction catalysed: 
ATP + a long-chain fatty acid + an [acyl-carrier-protein] = AMP + diphosphate + a long-chain acyl-[acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109582 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Long-chain-fatty-acid--AMP ligase FadD32 Chains: A, B
Molecule details ›
Chains: A, B
Length: 629 amino acids
Theoretical weight: 68.97 KDa
Source organism: Mycobacterium marinum
Expression system: Escherichia coli
UniProt:
  • Canonical: B2HMK0 (Residues: 1-629; Coverage: 100%)
Gene names: MMAR_5365, fadD32
Sequence domains: AMP-binding enzyme

Ligands and Environments

2 bound ligands:
Ligand 5SV 2 x 5SV
Ligand GOL 7 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 71.79Å b: 100.15Å c: 212.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.238
Expression system: Escherichia coli

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Citations

11 citation in other articles

Mycobacterium marinum Degrades Both Triacylglycerols and Phospholipids from Its Dictyostelium Host to Synthesise Its Own Triacylglycerols and Generate Lipid Inclusions.
Barisch et al. (2017)
10 more

2 mentions without citation

Structure of the Essential Mtb FadD32 Enzyme: A Promising Drug Target for Treating Tuberculosis.
Kuhn et al. (2016)
1 more