2fq0

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[[Image:2fq0.gif|left|200px]]<br /><applet load="2fq0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fq0.gif|left|200px]]
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caption="2fq0" />
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'''Solution structure of major conformation of holo-acyl carrier protein from malaria parasite plasmodium falciparum'''<br />
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{{Structure
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|PDB= 2fq0 |SIZE=350|CAPTION= <scene name='initialview01'>2fq0</scene>
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|SITE=
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|LIGAND= <scene name='pdbligand=PNS:4'-PHOSPHOPANTETHEINE'>PNS</scene>
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|ACTIVITY=
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|GENE= malaria parasite P. falciparum ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum])
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}}
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'''Solution structure of major conformation of holo-acyl carrier protein from malaria parasite plasmodium falciparum'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2FQ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with <scene name='pdbligand=PNS:'>PNS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQ0 OCA].
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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].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16734426 16734426]
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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]
[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: holo-pfacp]]
[[Category: holo-pfacp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:55:30 2008''

Revision as of 14:55, 20 March 2008


PDB ID 2fq0

Drag the structure with the mouse to rotate
Ligands:
Gene: malaria parasite P. falciparum (Plasmodium falciparum)
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

2FQ0 is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.

Reference

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

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