› 2x2b

X-ray diffraction
2.69Å resolution

Crystal structure of malonyl-ACP (acyl carrier protein) from Bacillus subtilis

Released:
DOI: 10.2210/pdb2x2b/pdb
PDB entry 2x2b coloured by chain, front view.
PDB entry 2x2b coloured by chain, side view.
PDB entry 2x2b coloured by chain, top view.
Source organism: Bacillus subtilis subsp. subtilis str. 168
Primary publication:
A novel role of malonyl-ACP in lipid homeostasis.
Martinez MA, Zaballa ME, Schaeffer F, Bellinzoni M, Albanesi D, Schujman GE, Vila AJ, Alzari PM, de Mendoza D
Biochemistry 49 3161-7 (2010)
PMID: 20201588

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160436 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl carrier protein Chain: A
Molecule details ›
Chain: A
Length: 78 amino acids
Theoretical weight: 8.65 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P80643 (Residues: 1-77; Coverage: 100%)
Gene names: BSU15920, acpA, acpP
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

2 bound ligands:
Ligand SXM 1 x SXM
Ligand PT 2 x PT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I4122
Unit cell:
a: 96.944Å b: 96.944Å c: 98.816Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.212 0.233
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Current understanding of fatty acid biosynthesis and the acyl carrier protein.
Chan et al. (2010)
6 more

3 mentions without citation

The crystal structure of BlmI as a model for nonribosomal peptide synthetase peptidyl carrier proteins.
Lohman et al. (2014)
2 more