2fve: Difference between revisions
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[[Image:2fve.gif|left|200px]] | [[Image:2fve.gif|left|200px]] | ||
'''Structure of 10:0-ACP (protein alone)''' | {{Structure | ||
|PDB= 2fve |SIZE=350|CAPTION= <scene name='initialview01'>2fve</scene> | |||
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|LIGAND= | |||
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'''Structure of 10:0-ACP (protein alone)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2FVE is a [ | 2FVE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVE OCA]. | ||
==Reference== | ==Reference== | ||
Solution structures of spinach acyl carrier protein with decanoate and stearate., Zornetzer GA, Fox BG, Markley JL, Biochemistry. 2006 Apr 25;45(16):5217-27. PMID:[http:// | Solution structures of spinach acyl carrier protein with decanoate and stearate., Zornetzer GA, Fox BG, Markley JL, Biochemistry. 2006 Apr 25;45(16):5217-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16618110 16618110] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Spinacia oleracea]] | [[Category: Spinacia oleracea]] | ||
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[[Category: 4-helix bundle]] | [[Category: 4-helix bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:57:14 2008'' | ||
Revision as of 17:57, 20 March 2008
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Structure of 10:0-ACP (protein alone)
OverviewOverview
Acyl carrier protein (ACP) is a cofactor in a variety of biosynthetic pathways, including fatty acid metabolism. Thus, it is of interest to determine structures of physiologically relevant ACP-fatty acid complexes. We report here the NMR solution structures of spinach ACP with decanoate (10:0-ACP) and stearate (18:0-ACP) attached to the 4'-phosphopantetheine prosthetic group. The protein in the fatty acid complexes adopts a single conformer, unlike apo- and holo-ACP, which interconvert in solution between two major conformers. The protein component of both 10:0- and 18:0-ACP adopts the four-helix bundle topology characteristic of ACP, and a fatty acid binding cavity was identified in both structures. Portions of the protein close in space to the fatty acid and the 4'-phosphopantetheine were identified using filtered/edited NOESY experiments. A docking protocol was used to generate protein structures containing bound fatty acid for 10:0- and 18:0-ACP. In both cases, the predominant structure contained fatty acid bound down the center of the helical bundle, in agreement with the location of the fatty acid binding pockets. These structures demonstrate the conformational flexibility of spinach ACP and suggest how the protein changes to accommodate its myriad binding partners.
About this StructureAbout this Structure
2FVE is a Single protein structure of sequence from Spinacia oleracea. Full crystallographic information is available from OCA.
ReferenceReference
Solution structures of spinach acyl carrier protein with decanoate and stearate., Zornetzer GA, Fox BG, Markley JL, Biochemistry. 2006 Apr 25;45(16):5217-27. PMID:16618110
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