Acyl carrier protein

Acyl/peptidyl carrier protein
Streptomyces coelicolor actinorhodin polyketide synthase acyl carrier protein - PDB: 2AF8​
Identifiers
SymbolACP-like_sf
PfamPF00550
Pfam clanCL0314
InterProIPR036736
PROSITEPDOC00012
CATH1nq4
SCOP21nq4 / 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 acyl carrier protein synthase (ACPS), a 4'-phosphopantetheinyl transferase. 4'-Phosphopantetheine is a prosthetic group of several acyl carrier proteins including the acyl carrier proteins (ACP) of fatty acid synthases, ACPs of polyketide synthases, the peptidyl carrier proteins (PCP), as well as aryl carrier proteins (ArCP) of nonribosomal peptide synthetases (NRPS).

References

  1. ^ Cronan, John E. (2014). "The Chain-Flipping Mechanism of ACP (Acyl Carrier Protein)-Dependent enzymes Appears Universal". Biochemical Journal. 460 (2): 157–163. doi:10.1042/BJ20140239. PMID 24825445.
  2. ^ Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB (June 2002). "X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site". Structure. 10 (6). London, England: 825–35. doi:10.1016/s0969-2126(02)00775-x. PMID 12057197.
  3. ^ Crawford JM, Vagstad AL, Ehrlich KC, Udwary DW, Townsend CA (July 2008). "Acyl-carrier protein-phosphopantetheinyltransferase partnerships in fungal fatty acid synthases". ChemBioChem. 9 (10): 1559–63. doi:10.1002/cbic.200700659. PMC 3189688. PMID 18551496.
  4. ^ Volkman BF, Zhang Q, Debabov DV, Rivera E, Kresheck GC, Neuhaus FC (July 2001). "Biosynthesis of D-alanyl-lipoteichoic acid: the tertiary structure of apo-D-alanyl carrier protein". Biochemistry. 40 (27): 7964–72. doi:10.1021/bi010355a. PMID 11434765.
  5. ^ Weber T, Baumgartner R, Renner C, Marahiel MA, Holak TA (April 2000). "Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases". Structure. 8 (4): 407–18. doi:10.1016/s0969-2126(00)00120-9. PMID 10801488.