› 2h1y

X-ray diffraction
2.5Å resolution

Crystal structure of malonyl-CoA:Acyl carrier protein transacylase (MCAT) from Helicobacter pylori

Released:
DOI: 10.2210/pdb2h1y/pdb
PDB entry 2h1y coloured by chain, front view.
PDB entry 2h1y coloured by chain, side view.
PDB entry 2h1y coloured by chain, top view.
Source organism: Helicobacter pylori SS1
Primary publication:
Malonyl-CoA: acyl carrier protein transacylase from Helicobacter pylori: Crystal structure and its interaction with acyl carrier protein.
Zhang L, Liu W, Xiao J, Hu T, Chen J, Chen K, Jiang H, Shen X
Protein Sci 16 1184-92 (2007)
PMID: 17525466

Function and Biology Details

Reaction catalysed: 
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[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-176393 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malonyl CoA-acyl carrier protein transacylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 321 amino acids
Theoretical weight: 35.8 KDa
Source organism: Helicobacter pylori SS1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56S05 (Residues: 1-309; Coverage: 100%)
Gene name: fabD
Sequence domains: Acyl transferase domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 43.616Å b: 76.175Å c: 99.768Å
α: 90° β: 101.22° γ: 90°
R-values:
R R work R free
0.217 0.215 0.262
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The structural role of the carrier protein--active controller or passive carrier.
Crosby et al. (2012)
4 more

4 mentions without citation

Using modern tools to probe the structure-function relationship of fatty acid synthases.
Finzel et al. (2015)
3 more