› 2ref

X-ray diffraction
2.75Å resolution

Crystal structure of the loading GNATL domain of CurA from Lyngbya majuscula soaked with malonyl-CoA

Released:
DOI: 10.2210/pdb2ref/pdb
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PDB entry 2ref coloured by chain, front view.
PDB entry 2ref coloured by chain, side view.
PDB entry 2ref coloured by chain, top view.
Source organism: Moorena producens 19L
Primary publication:
GNAT-like strategy for polyketide chain initiation.
Gu L, Geders TW, Wang B, Gerwick WH, Håkansson K, Smith JL, Sherman DH
Science 318 970-4 (2007)
PMID: 17991863

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]
Malonyl-CoA = acetyl-CoA + CO(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179535 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CurA Chains: A, B
Molecule details ›
Chains: A, B
Length: 224 amino acids
Theoretical weight: 25.91 KDa
Source organism: Moorena producens 19L
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6DNF2 (Residues: 219-439; Coverage: 10%)
Gene name: curA
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand ACO 2 x ACO
No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P3121
Unit cell:
a: 91.886Å b: 91.886Å c: 139.486Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.207 0.251
Expression system: Escherichia coli BL21(DE3)

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Citations

17 review citations

Biosynthesis of polyketides by trans-AT polyketide synthases.
Piel J. (2010)
16 more

5 mentions without citation

The Uncommon Enzymology of Cis-Acyltransferase Assembly Lines.
Keatinge-Clay AT. (2017)
4 more

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