2fve: Difference between revisions

Revision as of 15:30, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fve.png

Template:STRUCTURE 2fve

Structure of 10:0-ACP (protein alone)Structure of 10:0-ACP (protein alone)

Template:ABSTRACT PUBMED 16618110

About this StructureAbout this Structure

2FVE is a Single protein structure of sequence from Spinacia oleracea. Full experimental 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2fve|  PDB=2fve  |  SCENE=  }}
-'''Structure of 10:0-ACP (protein alone)'''
+===Structure of 10:0-ACP (protein alone)===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16618110}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16618110 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16618110}}
 ==About this Structure==
-FVE 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].
+FVE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVE OCA].
 ==Reference==
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 [[Category: Zornetzer, G A.]]
 [[Category: 4-helix bundle]]
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