Acyl carrier protein
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<scene name='59/592131/Cv/6'>Active site</scene> of ''E. coli'' acyl carrier protein ([[2fad]]). | <scene name='59/592131/Cv/6'>Active site</scene> of ''E. coli'' acyl carrier protein ([[2fad]]). | ||
| - | The <scene name='59/592131/Cv/ | + | The <scene name='59/592131/Cv/7'>thioester - heptanethioate - is bound to ACP serine residue</scene> (colored in darkmagenta) in an expandable hydrophobic cavity.<ref>PMID:17059829</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 13:51, 23 April 2018
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3D structures of acyl carrier protein
Updated on 23-April-2018
References
- ↑ 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
- ↑ 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
