 |
InterPro: IPR003231 Acyl carrier protein (ACP)
Protein matches
|
UniProtKB Matches: 2240 proteins |
|
Accession
|
IPR003231 Acyl_carrier |
Secondary
|
IPR003880
|
Type
|
Family |
Signatures
|
|
InterPro Relationships
|
|
Parent
|
IPR006163 Phosphopantetheine-binding
|
|
Contains
|
IPR006162 Phosphopantetheine attachment site
|
GO Term annotation
|
|
Process
|
GO:0006633 fatty acid biosynthetic process
|
|
Function
|
GO:0000036 acyl carrier activity
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
There are two types of fatty acid synthase systems. The type I system is found in metazoans and is carried out
by a multifunctional polypeptide with multiple active sites. In contrast, the type II system found in bacteria and plants
consists of a set of discrete monofunctional proteins, each encoded by a separate gene. ACP1 is central to both of these
pathways because it functions to ferry the pathway intermediates between active site centres or enzymes. ACPs are also
critical to the function of other metabolic pathways such as polyketide synthases.
The type II fatty acid synthase ACPs are abundant, small, acidic proteins that carry the acyl intermediates attached as thioesters to the terminus of the 4'-phosphopantetheine prosthetic group. This prosthetic group is added post-translationally to apoACP by holo-(acyl carrier protein) synthase (AcpS), which transfers the 4'-phosphopantetheine moiety of CoA to a serine reidue of apoACP.
The crystal structures of a number of the type II fatty acid synthase ACPs have been determined. The structures reveal a novel trimeric arrangement of molecules resulting in three active sites [1, 2].
|
Structural links
|
|
Publications
|
|
1.
|
Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS.
Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites.
Structure 8 883-95 2000
[PubMed: 10997907]
http://dx.doi.org/10.1016/S0969-2126(00)00178-7
|
|
2.
|
Findlow SC, Winsor C, Simpson TJ, Crosby J, Crump MP.
Solution structure and dynamics of oxytetracycline polyketide synthase acyl carrier protein from Streptomyces rimosus.
Biochemistry 42 8423-33 2003
[PubMed: 12859187]
http://dx.doi.org/10.1021/bi0342259
|
Additional Reading
|
|
Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR.
Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates.
J. Mol. Biol. 365 2007 135-45
[PubMed: 17059829]
http://dx.doi.org/10.1016/j.jmb.2006.09.049
|
|
Rafi S, Novichenok P, Kolappan S, Zhang X, Stratton CF, Rawat R, Kisker C, Simmerling C, Tonge PJ.
Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli.
J. Biol. Chem. 281 2006 39285-93
[PubMed: 17012233]
http://dx.doi.org/10.1074/jbc.M608758200
|
|
Zornetzer GA, Fox BG, Markley JL.
Solution structures of spinach acyl carrier protein with decanoate and stearate.
Biochemistry 45 2006 5217-27
[PubMed: 16618110]
http://dx.doi.org/10.1021/bi052062d
|
|
Cryle MJ, Schlichting I.
Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 15696-701
[PubMed: 18838690]
http://dx.doi.org/10.1073/pnas.0805983105
|
|
Sharma AK, Sharma SK, Surolia A, Surolia N, Sarma SP.
Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs.
Biochemistry 45 2006 6904-16
[PubMed: 16734426]
http://dx.doi.org/10.1021/bi060368u
|
|
|
InterPro 23.1
|