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2fq0

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Revision as of 09:24, 14 June 2018

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

Structural highlights

2fq0 is a 1 chain structure with sequence from Plaf7. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2bar, 2fq3
Gene:	malaria parasite P. falciparum (PLAF7)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[O77077_PLAFA] Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity).[RuleBase:RU000722]

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) 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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sharma AK, Sharma SK, Surolia A, Surolia N, Sarma SP. Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs. Biochemistry. 2006 Jun 6;45(22):6904-16. PMID:16734426 doi:10.1021/bi060368u

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fq0"

@@ Line 1: / Line 1: @@
 ==Solution structure of major conformation of holo-acyl carrier protein from malaria parasite plasmodium falciparum==
 <StructureSection load='2fq0' size='340' side='right' caption='[[2fq0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bar|2bar]], [[2fq3|2fq3]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malaria parasite P. falciparum ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</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=2fq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fq0 OCA], [http://pdbe.org/2fq0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fq0 RCSB], [http://www.ebi.ac.uk/pdbsum/2fq0 PDBsum]</span></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=2fq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fq0 OCA], [http://pdbe.org/2fq0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fq0 RCSB], [http://www.ebi.ac.uk/pdbsum/2fq0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fq0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/2fq0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/2fq0_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2fq0

From Proteopedia

Revision as of 09:24, 14 June 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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