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| {{STRUCTURE_2fac| PDB=2fac | SCENE= }} | | {{STRUCTURE_2fac| PDB=2fac | SCENE= }} |
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| '''Crystal structure of E. coli hexanoyl-ACP'''
| | ===Crystal structure of E. coli hexanoyl-ACP=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17059829}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17059829 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17059829}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Acyl chain binding]] | | [[Category: Acyl chain binding]] |
| [[Category: Fatty acid biosynthesis]] | | [[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 Mon Jul 28 20:37:51 2008'' |
