Jump to content

Acyl carrier protein

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Neutronstar2 (talk | contribs) at 09:22, 15 July 2020 (→‎External links: readability cleanup). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

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 an important component in both fatty acid and polyketide biosynthesis with the growing chain bound during synthesis as a thiol ester at the distal thiol of a 4'-phosphopantetheine moiety. The ACPs are related in structure and mechanism to the peptidyl carrier proteins (PCP) from nonribosomal peptide synthases.

The protein is expressed in the inactive apo form and the 4'-phosphopantetheine moiety must be post-translationally attached to a conserved serine residue on the ACP by the action of holo-acyl carrier protein synthase (ACPS), a 4'-phosphopantetheinyl transferase. 4'-Phosphopantetheine is an essential prosthetic group of several acyl carrier proteins involved in pathways of primary and secondary metabolism including the acyl carrier proteins (ACP) of fatty acid synthases, ACPs of polyketide synthases, and peptidyl carrier proteins (PCP) and aryl carrier proteins (ArCP) of nonribosomal peptide synthetases (NRPS). Phosphopantetheine fulfills two demands in these biosynthetic pathways. First, the intermediates remain covalently linked to the synthases (or synthetases) in an energy-rich linkage. Second, the flexibility and length of the phosphopantetheine chain (approximately 2 nm) allows the covalently tethered intermediates to have access to spatially distinct enzyme-active sites. This increases the effective molarity of the intermediate and allows an assembly line-like process.

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.

External links