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| - | [[Image:2ok7.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2ok7.png|left|200px]] |
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| | {{STRUCTURE_2ok7| PDB=2ok7 | SCENE= }} | | {{STRUCTURE_2ok7| PDB=2ok7 | SCENE= }} |
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| - | '''Ferredoxin-NADP+ reductase from Plasmodium falciparum with 2'P-AMP'''
| + | ===Ferredoxin-NADP+ reductase from Plasmodium falciparum with 2'P-AMP=== |
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| - | ==Overview==
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| - | The completion of the Plasmodium falciparum genome sequence has recently promoted the search for new antimalarial drugs. More specifically, metabolic pathways of the apicoplast, a key organelle for survival of the parasite, have been recognized as potential targets for the development of specific new antimalarial agents. As most apicomplexan parasites, P. falciparum displays a plant-type ferredoxin-NADP(+) reductase, yielding reduced ferredoxin for essential biosynthetic pathways in the apicoplast. Here we report a molecular, kinetic and ligand binding characterization of the recombinant ferredoxin-NADP(+) reductase from P. falciparum, in the light of current data available for plant ferredoxin-NADP(+) reductases. In parallel with the functional characterization, we describe the crystal structures of P. falciparum ferredoxin-NADP(+) reductase in free form and in complex with 2'-phospho-AMP (at 2.4 and 2.7 A resolution, respectively). The enzyme displays structural properties likely to be unique to plasmodial reductases. In particular, the two crystal structures highlight a covalent dimer, which relies on the oxidation of residue Cys99 in two opposing subunits, and a helix-coil transition that occurs in the NADP-binding domain, triggered by 2'-phospho-AMP binding. Studies in solution show that NADP(+), as well as 2'-phospho-AMP, promotes the formation of the disulfide-stabilized dimer. The isolated dimer is essentially inactive, but full activity is recovered upon disulfide reduction. The occurrence of residues unique to the plasmodial enzyme, and the discovery of specific conformational properties, highlight the NADP-binding domain of P. falciparum ferredoxin-NADP(+) reductase as particularly suited for the rational development of antimalarial compounds. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17258767}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17258767 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17258767}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Milani, M.]] | | [[Category: Milani, M.]] |
| | [[Category: Disulfide-stabilized dimer]] | | [[Category: Disulfide-stabilized dimer]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:04:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:54:48 2008'' |
Revision as of 18:54, 27 July 2008
Template:STRUCTURE 2ok7
Ferredoxin-NADP+ reductase from Plasmodium falciparum with 2'P-AMP
Template:ABSTRACT PUBMED 17258767
About this Structure
2OK7 is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
Reference
Ferredoxin-NADP+ reductase from Plasmodium falciparum undergoes NADP+-dependent dimerization and inactivation: functional and crystallographic analysis., Milani M, Balconi E, Aliverti A, Mastrangelo E, Seeber F, Bolognesi M, Zanetti G, J Mol Biol. 2007 Mar 23;367(2):501-13. Epub 2007 Jan 9. PMID:17258767
Page seeded by OCA on Sun Jul 27 21:54:48 2008
