Acyl carrier protein

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<StructureSection load='' size='350' side='right' caption='Structure of E. coli acyl carrier protein complex with thioester, Zn+2 (grey) and Na+ (purple) ions (PDB code [[2fad]]).' scene='59/592131/Cv/1'>
<StructureSection load='' size='350' side='right' caption='Structure of E. coli acyl carrier protein complex with thioester, Zn+2 (grey) and Na+ (purple) ions (PDB code [[2fad]]).' scene='59/592131/Cv/1'>
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__TOC__
== Function ==
== Function ==
'''Acyl carrier protein''' (ACP) is a component of the fatty acid biosynthesis cycle. ACP catalyzes the addition of a thioester to a phosphopantetheine moiety. The phosphopantetheine moiety is added post-translationally to ACP serine residue by ACP synthetase (ACPS). The phosphopantetheine contains a free SH group which binds acyl groups in the fatty acid biosynthesis as thioesters. The acyl groups from acetyl-CoA and malonyl-CoA are transferred to ACP. There are 2 types of ACP. '''ACP I''' is a multifunctional polypeptide found in yeast and mammals while '''ACP II''' is a monomeric protein found in bacteria and plants.<ref>PMID:18059524</ref>
'''Acyl carrier protein''' (ACP) is a component of the fatty acid biosynthesis cycle. ACP catalyzes the addition of a thioester to a phosphopantetheine moiety. The phosphopantetheine moiety is added post-translationally to ACP serine residue by ACP synthetase (ACPS). The phosphopantetheine contains a free SH group which binds acyl groups in the fatty acid biosynthesis as thioesters. The acyl groups from acetyl-CoA and malonyl-CoA are transferred to ACP. There are 2 types of ACP. '''ACP I''' is a multifunctional polypeptide found in yeast and mammals while '''ACP II''' is a monomeric protein found in bacteria and plants.<ref>PMID:18059524</ref>
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See also [[Molecular Playground/ACP apo]]
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See also:
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*[[Molecular Playground/ACP apo]]
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*[[Acyl carrier protein synthase]]
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*[[Lipid metabolism]]
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*[[Fatty acid synthesis]]
== Structural highlights ==
== Structural highlights ==
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The <scene name='59/592131/Cv/10'>thioester - heptanethioate - is bound to ACP serine residue</scene> (colored in darkmagenta) in an expandable hydrophobic cavity.<ref>PMID:17059829</ref>
The <scene name='59/592131/Cv/10'>thioester - heptanethioate - is bound to ACP serine residue</scene> (colored in darkmagenta) in an expandable hydrophobic cavity.<ref>PMID:17059829</ref>
*<scene name='59/592131/Cv/15'>Na coordination site</scene>.
*<scene name='59/592131/Cv/15'>Na coordination site</scene>.
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*<scene name='59/592131/Cv/12'>Active site hydrophobic cavity with thioester heptanethioate</scene>.
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*<scene name='59/592131/Cv/16'>Active site hydrophobic cavity with thioester heptanethioate</scene>.
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</StructureSection>
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==3D structures of acyl carrier protein==
==3D structures of acyl carrier protein==
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[[Acyl carrier protein 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Acyl carrier protein
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**[[1l0h]], [[1t8k]] – EcACP – ''Escherichia coli'' <br />
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**[[1l0i]] – EcACP (mutant)<br />
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**[[1hy8]] – BsACP – ''Bacillus subtilis''<br />
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**[[1vku]] – ACP – ''Thermotoga maritima''<br />
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**[[1x3o]] – ACP – ''Thermus thermophilus''<br />
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**[[2fq0]], [[3gzl]], [[3gzm]] – PfACP – ''Plasmodium falciparum''<br />
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**[[2qnw]] – ACP residues 100-180 – ''Toxoplasma gondii''<br />
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**[[2ehs]], [[2eht]] – ACP – ''Aquifex aeolicus''<br />
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**[[3ce7]] – ACP – ''Toxoplasma'' <br />
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**[[5h9g]], [[5h9h]] – HpACP – ''Helicobacter pylori''<br />
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*Acyl carrier protein NMR structures
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**[[2kwl]] – ACP – ''Borrelia burgdorferi'' - NMR <br />
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**[[2l0q]] – ACP (mutant) – ''Vibrio harveyi'' - NMR<br />
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**[[2n57]] – ACP – ''Brucella melitensis'' - NMR <br />
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**[[2l4b]] – ACP – ''Anaplasma phagocytophilum'' - NMR <br />
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**[[2lol]] – ACP – ''Rickettsia prowazekii'' - NMR <br />
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**[[1acp]], [[2k92]], [[2k93]], [[2k94]] – EcACP - NMR<br />
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**[[1or5]] – ACP – ''Streptomyces roseofulvus'' - NMR<br />
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**[[2fq2]] – PfACP - NMR<br />
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**[[2cnr]] – ScACP – ''Streptomyces coelicolor'' - NMR<br />
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**[[2n98]] – ACP – ''Actinoplanes friulensis'' - NMR<br />
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**[[2n50]] – ACP – ''Enterococcus faecalis'' - NMR<br />
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*Acyl carrier protein complex with fatty acid
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**[[2fac]], [[2fad]], [[2fae]] – EcACP + thioester <br />
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**[[2koo]], [[2kop]], [[2koq]], [[2kor]], [[2kos]] – ScACP + thioester - NMR<br />
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**[[2x2b]] – EcACP + malonate derivative <br />
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*Acyl carrier protein complex with protein
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**[[2fhs]] – EcACP + enoyl-[ACP] reductase <br />
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**[[3ejb]], [[3ejd]], [[3eje]] – EcACP + thioester + p450BioI<br />
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**[[3ny7]] – EcACP + YchM STAS domain <br />
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**[[5vcb]] – EcACP + holo-[ACP] synthase <br />
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**[[5kof]] – EcACP + oxoacyl-[ACP] synthase <br />
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**[[5wgb]], [[5usr]] – EcACP + cysteine desulferase + LYR motif-containing protein 4 <br />
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**[[5wlw]], [[5wkp]] – EcACP + cysteine desulferase + LYR motif-containing protein 4 + ISCU<br />
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**[[1f80]] – BsACP + ACPS <br />
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**[[4dxe]] – ACP + ACPS – ''Staphylococcus aureus''<br />
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**[[4etw]] – ACP + pimelyl-[ACP] methyl ester esterase – ''Shigella flexneri''<br />
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**[[4ihf]], [[4ihg]], [[4ihh]] – EcACP + protein FIRA <br />
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**[[4keh]] – EcACP + fatty acid dehydratase <br />
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**[[4zjb]] – HpACP + FabZ<br />
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**[[5czd]] – ACP + malonyl-CoA-ACP transacylase – ''Streptomyces halstedii''<br />
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Structure of E. coli acyl carrier protein complex with thioester, Zn+2 (grey) and Na+ (purple) ions (PDB code 2fad).

Drag the structure with the mouse to rotate

References

  1. ↑ Byers DM, Gong H. Acyl carrier protein: structure-function relationships in a conserved multifunctional protein family. Biochem Cell Biol. 2007 Dec;85(6):649-62. PMID:18059524 doi:http://dx.doi.org/10.1139/o07-109
  2. ↑ 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. 2007 Jan 5;365(1):135-45. Epub 2006 Sep 23. PMID:17059829 doi:10.1016/j.jmb.2006.09.049

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Alexander Berchansky, Michal Harel, Joel L. Sussman

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