2fae
From Proteopedia
(New page: 200px<br /> <applet load="2fae" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fae, resolution 1.550Å" /> '''Crystal structure ...) |
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| - | [[Image:2fae.gif|left|200px]]<br /> | + | [[Image:2fae.gif|left|200px]]<br /><applet load="2fae" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2fae, resolution 1.550Å" /> | caption="2fae, resolution 1.550Å" /> | ||
'''Crystal structure of E. coli decanoyl-ACP'''<br /> | '''Crystal structure of E. coli decanoyl-ACP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A knowledge of the structures of acyl chain loaded species of the acyl | + | 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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, PM8 and PSE as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 2FAE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=PM8:'>PM8</scene> and <scene name='pdbligand=PSE:'>PSE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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== | ==Reference== | ||
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[[Category: fatty acid biosynthesis]] | [[Category: fatty acid biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:26 2008'' |
Revision as of 15:19, 21 February 2008
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Crystal structure of E. coli decanoyl-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
2FAE is a Single protein structure of sequence from Escherichia coli with , and as ligands. The following page contains interesting information on the relation of 2FAE with [Fatty Acid Synthase]. 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
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