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2fad

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[[Image:2fad.gif|left|200px]]
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{{STRUCTURE_2fad| PDB=2fad | SCENE= }}
{{STRUCTURE_2fad| PDB=2fad | SCENE= }}
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'''Crystal structure of E. coli heptanoyl-ACP'''
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===Crystal structure of E. coli heptanoyl-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.
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The line below this paragraph, {{ABSTRACT_PUBMED_17059829}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 17059829 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17059829}}
==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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:39:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:15:43 2008''

Revision as of 22:15, 27 July 2008

Image:2fad.png

Template:STRUCTURE 2fad

Crystal structure of E. coli heptanoyl-ACP

Template:ABSTRACT PUBMED 17059829

About this Structure

2FAD 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 Mon Jul 28 01:15:43 2008

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