Acyl carrier protein

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Acyl/peptidyl carrier protein
SCOP2
1nq4 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The acyl carrier protein (ACP) is a cofactor of both fatty acid and polyketide biosynthesis machinery. It is one of the most abundant proteins in cells of E. coli.[1] In both cases, the growing chain is bound to the ACP via a thioester derived from the distal thiol of a 4'-phosphopantetheine moiety.

Structure

The ACPs are small negatively charged α-helical bundle proteins with a high degree of structural and amino acid similarity. The structures of a number of acyl carrier proteins have been solved using various

NMR and crystallography techniques. The ACPs are related in structure and mechanism to the peptidyl carrier proteins (PCP) from nonribosomal peptide synthases.[2][3][4][5]

Biosynthesis

Subsequent to the expression of the inactive apo ACP, the 4'-phosphopantetheine moiety is attached to a serine residue. This coupling is mediated by

nonribosomal peptide synthetases
(NRPS).

References

External links