2fae: Difference between revisions

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[[Image:2fae.gif|left|200px]]
[[Image:2fae.png|left|200px]]


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==Overview==
{{ABSTRACT_17059829}}
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==
==About this Structure==
2FAE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 2FAE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FAE OCA].  
2FAE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 2FAE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FAE 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:[http://www.ncbi.nlm.nih.gov/pubmed/17059829 17059829]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Fatty Acid Synthase]]
[[Category: Fatty Acid Synthase]]
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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 03:39:34 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 18:16:16 2008''

Revision as of 15:16, 26 June 2008

File:2fae.png

Template:STRUCTURE 2fae

Crystal structure of E. coli decanoyl-ACP


Template:ABSTRACT 17059829

About this Structure

2FAE is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 2FAE with [Fatty Acid Synthase]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 18:16:16 2008

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