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2fac
From Proteopedia
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[[Image:2fac.gif|left|200px]] | [[Image:2fac.gif|left|200px]] | ||
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'''Crystal structure of E. coli hexanoyl-ACP''' | '''Crystal structure of E. coli hexanoyl-ACP''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Roujeinikova, A.]] | [[Category: Roujeinikova, A.]] | ||
| - | [[Category: | + | [[Category: Acyl carrier protein]] |
| - | [[Category: | + | [[Category: Acyl chain binding]] |
| - | [[Category: | + | [[Category: Fatty acid biosynthesis]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:39:23 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:39, 4 May 2008
Crystal structure of E. coli hexanoyl-ACP
Overview
A knowledge of the structures of acyl chain loaded species of the acyl carrier protein (ACP) as used in fatty acid biosynthesis and a range of other metabolic events, is essential for a full understanding of the molecular recognition at the heart of these processes. To date the only crystal structure of an acylated species of ACP is that of a butyryl derivative of Escherichia coli ACP. We have now determined the structures of a family of acylated E. coli ACPs of varying acyl chain length. The acyl moiety is attached via a thioester bond to a phosphopantetheine linker that is in turn bound to a serine residue in ACP. The growing acyl chain can be accommodated within a central cavity in the ACP for transport during the elongation stages of lipid synthesis through changes in the conformation of a four alpha-helix bundle. The results not only clarify the means by which a substrate of varying size and complexity is transported in the cell but also suggest a mechanism by which interacting enzymes can recognize the loaded ACP through recognition of surface features including the conformation of the phosphopantetheine linker.
About this Structure
2FAC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates., Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR, J Mol Biol. 2007 Jan 5;365(1):135-45. Epub 2006 Sep 23. PMID:17059829 Page seeded by OCA on Sun May 4 03:39:23 2008
