2fva
From Proteopedia
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| - | [[Image:2fva.gif|left|200px]] | + | [[Image:2fva.gif|left|200px]] |
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| - | '''Structure of 18:0-ACP with docked fatty acid''' | + | {{Structure |
| + | |PDB= 2fva |SIZE=350|CAPTION= <scene name='initialview01'>2fva</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PNS:4'-PHOSPHOPANTETHEINE'>PNS</scene> and <scene name='pdbligand=STE:STEARIC ACID'>STE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of 18:0-ACP with docked fatty acid''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FVA is a [ | + | 2FVA 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=2FVA 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 16:57:07 2008'' |
Revision as of 14:57, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of 18:0-ACP with docked fatty acid
Overview
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 Structure
2FVA is a Single protein structure of sequence from Spinacia oleracea. Full crystallographic information is available from OCA.
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:16618110
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