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| | ==Structure of 10:0-ACP (protein alone)== | | ==Structure of 10:0-ACP (protein alone)== |
| - | <StructureSection load='2fve' size='340' side='right' caption='[[2fve]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2fve' size='340' side='right'caption='[[2fve]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fve]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spiol Spiol]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FVE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fve]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FVE FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ava|2ava]], [[2fva|2fva]], [[2fvf|2fvf]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fve OCA], [http://pdbe.org/2fve PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fve RCSB], [http://www.ebi.ac.uk/pdbsum/2fve PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fve ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fve OCA], [https://pdbe.org/2fve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fve RCSB], [https://www.ebi.ac.uk/pdbsum/2fve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fve ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACP1_SPIOL ACP1_SPIOL]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] | + | [https://www.uniprot.org/uniprot/ACP1_SPIOL ACP1_SPIOL] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Spiol]] | + | [[Category: Large Structures]] |
| - | [[Category: Fox, B G]] | + | [[Category: Spinacia oleracea]] |
| - | [[Category: Markley, J L]] | + | [[Category: Fox BG]] |
| - | [[Category: Zornetzer, G A]] | + | [[Category: Markley JL]] |
| - | [[Category: 4-helix bundle]] | + | [[Category: Zornetzer GA]] |
| - | [[Category: Biosynthetic protein]]
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| Structural highlights
Function
ACP1_SPIOL Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zornetzer GA, Fox BG, Markley JL. Solution structures of spinach acyl carrier protein with decanoate and stearate. Biochemistry. 2006 Apr 25;45(16):5217-27. PMID:16618110 doi:10.1021/bi052062d
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