2fva: Difference between revisions

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-{{Seed}}
-[[Image:2fva.png|left|200px]]
-<!--
+==Structure of 18:0-ACP with docked fatty acid==
-The line below this paragraph, containing "STRUCTURE_2fva", creates the "Structure Box" on the page.
+<StructureSection load='2fva' size='340' side='right'caption='[[2fva]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2fva]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spiol Spiol]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FVA FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene>, <scene name='pdbligand=STE:STEARIC+ACID'>STE</scene></td></tr>
--->
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ava|2ava]], [[2fve|2fve]], [[2fvf|2fvf]]</div></td></tr>
-{{STRUCTURE_2fva|  PDB=2fva  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fva OCA], [https://pdbe.org/2fva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fva RCSB], [https://www.ebi.ac.uk/pdbsum/2fva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fva ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/2fva_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fva ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===Structure of 18:0-ACP with docked fatty acid===
+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<ref>PMID:16618110</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16618110}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2fva" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16618110 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16618110}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-FVA 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=2FVA OCA].
+[[Category: Spiol]]
+[[Category: Fox, B G]]
-==Reference==
+[[Category: Markley, J L]]
-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: Zornetzer, G A]]
-[[Category: Single protein]]
-[[Category: Spinacia oleracea]]
-[[Category: Fox, B G.]]
-[[Category: Markley, J L.]]
-[[Category: Zornetzer, G A.]]
 [[Category: 4-helix bundle]]
+[[Category: Biosynthetic protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:07:29 2008''