2fq0

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[[Image:2fq0.gif|left|200px]]
 
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==Solution structure of major conformation of holo-acyl carrier protein from malaria parasite plasmodium falciparum==
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The line below this paragraph, containing "STRUCTURE_2fq0", creates the "Structure Box" on the page.
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<StructureSection load='2fq0' size='340' side='right'caption='[[2fq0]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2fq0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FQ0 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></td></tr>
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{{STRUCTURE_2fq0| PDB=2fq0 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fq0 OCA], [https://pdbe.org/2fq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fq0 RCSB], [https://www.ebi.ac.uk/pdbsum/2fq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fq0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O77077_PLAFA O77077_PLAFA] Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity).[RuleBase:RU000722]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/2fq0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2fq0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Acyl Carrier Protein (ACP) from the malaria parasite, Plasmodium falciparum (PfACP) in its holo form is found to exist in two conformational states in solution. Unique 3D solution structures of holo-PfACP have been determined for both equilibrium conformations, using high-resolution NMR methods. Twenty high-resolution solution structures for each of the two forms of holo-PfACP have been determined on the basis of 1226 and 1218 unambiguously assigned NOEs (including NOEs between 4'-phosphopantetheine prosthetic group (4'-PP) and protein), 55 backbone dihedral angles and 26 hydrogen bonds. The atomic rmsd values of the determined structures of two equilibrium forms, about the mean coordinates of the backbone and heavy atoms, are 0.48 +/- 0.09 and 0.92 +/- 0.10 and 0.49 +/- 0.08 and 0.97 +/- 0.11 A, respectively. The interaction of 4'-PP with the polypeptide backbone is reported here for the first time for any of the ACPs. The structures of holo-PfACP consist of three well-defined helices that are tightly packed. The structured regions of the molecule are stabilized by extensive hydrophobic interactions. The difference between the two forms arises from a reorientation of the 4'-PP group. The enthalpy difference between the two forms, although small, implies that a conformational switch is essential for the activation of holo-ACP. Sequence and structures of holo-PfACP have been compared with those of the ACPs from type I and type II fatty acid biosynthesis pathways (FAS), in particular with the ACP from rat and the butyryl-ACP from E. coli. The PfACP structure, thus determined has several novel features hitherto not seen in other ACPs.
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'''Solution structure of major conformation of holo-acyl carrier protein from malaria parasite plasmodium falciparum'''
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Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs.,Sharma AK, Sharma SK, Surolia A, Surolia N, Sarma SP Biochemistry. 2006 Jun 6;45(22):6904-16. PMID:16734426<ref>PMID:16734426</ref>
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==Overview==
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Acyl Carrier Protein (ACP) from the malaria parasite, Plasmodium falciparum (PfACP) in its holo form is found to exist in two conformational states in solution. Unique 3D solution structures of holo-PfACP have been determined for both equilibrium conformations, using high-resolution NMR methods. Twenty high-resolution solution structures for each of the two forms of holo-PfACP have been determined on the basis of 1226 and 1218 unambiguously assigned NOEs (including NOEs between 4'-phosphopantetheine prosthetic group (4'-PP) and protein), 55 backbone dihedral angles and 26 hydrogen bonds. The atomic rmsd values of the determined structures of two equilibrium forms, about the mean coordinates of the backbone and heavy atoms, are 0.48 +/- 0.09 and 0.92 +/- 0.10 and 0.49 +/- 0.08 and 0.97 +/- 0.11 A, respectively. The interaction of 4'-PP with the polypeptide backbone is reported here for the first time for any of the ACPs. The structures of holo-PfACP consist of three well-defined helices that are tightly packed. The structured regions of the molecule are stabilized by extensive hydrophobic interactions. The difference between the two forms arises from a reorientation of the 4'-PP group. The enthalpy difference between the two forms, although small, implies that a conformational switch is essential for the activation of holo-ACP. Sequence and structures of holo-PfACP have been compared with those of the ACPs from type I and type II fatty acid biosynthesis pathways (FAS), in particular with the ACP from rat and the butyryl-ACP from E. coli. The PfACP structure, thus determined has several novel features hitherto not seen in other ACPs.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2FQ0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQ0 OCA].
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</div>
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<div class="pdbe-citations 2fq0" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs., Sharma AK, Sharma SK, Surolia A, Surolia N, Sarma SP, Biochemistry. 2006 Jun 6;45(22):6904-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16734426 16734426]
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*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]]
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[[Category: Plasmodium falciparum]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Sarma, S P.]]
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__TOC__
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[[Category: Sharma, A K.]]
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</StructureSection>
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[[Category: Sharma, S K.]]
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[[Category: Large Structures]]
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[[Category: Surolia, A.]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: Surolia, N.]]
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[[Category: Sarma SP]]
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[[Category: 4'-phosphopantetheine]]
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[[Category: Sharma AK]]
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[[Category: Holo-pfacp]]
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[[Category: Sharma SK]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:11:17 2008''
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[[Category: Surolia A]]
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[[Category: Surolia N]]

Current revision

Solution structure of major conformation of holo-acyl carrier protein from malaria parasite plasmodium falciparum

PDB ID 2fq0

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