1p9b

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(New page: 200px<br /><applet load="1p9b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9b, resolution 2.00&Aring;" /> '''Structure of fully l...)
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caption="1p9b, resolution 2.00&Aring;" />
'''Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum'''<br />
'''Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum'''<br />
==Overview==
==Overview==
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In the absence of the de novo purine nucleotide biosynthetic pathway in, parasitic protozoa, purine salvage is of primary importance for parasite, survival. Enzymes of the salvage pathway are, therefore, good targets for, anti-parasitic drugs. Adenylosuccinate synthetase (AdSS), catalysing the, first committed step in the synthesis of AMP from IMP, is a potential, target for anti-protozoal chemotherapy. We report here the crystal, structure of adenylosuccinate synthetase from the malaria parasite, Plasmodium falciparum, complexed to 6-phosphoryl IMP, GDP, Mg2+ and the, aspartate analogue, hadacidin at 2 A resolution. The overall architecture, of P. falciparum AdSS (PfAdSS) is similar to the known structures from, Escherichia coli, mouse and plants. Differences in substrate interactions, seen in this structure provide a plausible explanation for the kinetic, differences between PfAdSS and the enzyme from other species. Additional, hydrogen bonding interactions of the protein with GDP may account for the, ordered binding of substrates to the enzyme. The dimer interface of PfAdSS, is also different, with a pronounced excess of positively charged, residues. Differences highlighted here provide a basis for the design of, species-specific inhibitors of the enzyme.
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In the absence of the de novo purine nucleotide biosynthetic pathway in parasitic protozoa, purine salvage is of primary importance for parasite survival. Enzymes of the salvage pathway are, therefore, good targets for anti-parasitic drugs. Adenylosuccinate synthetase (AdSS), catalysing the first committed step in the synthesis of AMP from IMP, is a potential target for anti-protozoal chemotherapy. We report here the crystal structure of adenylosuccinate synthetase from the malaria parasite, Plasmodium falciparum, complexed to 6-phosphoryl IMP, GDP, Mg2+ and the aspartate analogue, hadacidin at 2 A resolution. The overall architecture of P. falciparum AdSS (PfAdSS) is similar to the known structures from Escherichia coli, mouse and plants. Differences in substrate interactions seen in this structure provide a plausible explanation for the kinetic differences between PfAdSS and the enzyme from other species. Additional hydrogen bonding interactions of the protein with GDP may account for the ordered binding of substrates to the enzyme. The dimer interface of PfAdSS is also different, with a pronounced excess of positively charged residues. Differences highlighted here provide a basis for the design of species-specific inhibitors of the enzyme.
==About this Structure==
==About this Structure==
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1P9B 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 MG, NO3, IMO, HDA and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P9B OCA].
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1P9B 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=MG:'>MG</scene>, <scene name='pdbligand=NO3:'>NO3</scene>, <scene name='pdbligand=IMO:'>IMO</scene>, <scene name='pdbligand=HDA:'>HDA</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9B OCA].
==Reference==
==Reference==
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[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Anand, R.P.]]
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[[Category: Anand, R P.]]
[[Category: Balaram, H.]]
[[Category: Balaram, H.]]
[[Category: Eaazhisai, K.]]
[[Category: Eaazhisai, K.]]
[[Category: Gayathri, P.]]
[[Category: Gayathri, P.]]
[[Category: Jayalakshmi, R.]]
[[Category: Jayalakshmi, R.]]
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[[Category: Murthy, M.R.]]
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[[Category: Murthy, M R.]]
[[Category: Sumathy, K.]]
[[Category: Sumathy, K.]]
[[Category: GDP]]
[[Category: GDP]]
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[[Category: ligase]]
[[Category: ligase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:12:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:40 2008''

Revision as of 12:26, 21 February 2008


1p9b, resolution 2.00Å

Drag the structure with the mouse to rotate

Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum

Overview

In the absence of the de novo purine nucleotide biosynthetic pathway in parasitic protozoa, purine salvage is of primary importance for parasite survival. Enzymes of the salvage pathway are, therefore, good targets for anti-parasitic drugs. Adenylosuccinate synthetase (AdSS), catalysing the first committed step in the synthesis of AMP from IMP, is a potential target for anti-protozoal chemotherapy. We report here the crystal structure of adenylosuccinate synthetase from the malaria parasite, Plasmodium falciparum, complexed to 6-phosphoryl IMP, GDP, Mg2+ and the aspartate analogue, hadacidin at 2 A resolution. The overall architecture of P. falciparum AdSS (PfAdSS) is similar to the known structures from Escherichia coli, mouse and plants. Differences in substrate interactions seen in this structure provide a plausible explanation for the kinetic differences between PfAdSS and the enzyme from other species. Additional hydrogen bonding interactions of the protein with GDP may account for the ordered binding of substrates to the enzyme. The dimer interface of PfAdSS is also different, with a pronounced excess of positively charged residues. Differences highlighted here provide a basis for the design of species-specific inhibitors of the enzyme.

About this Structure

1P9B is a Single protein structure of sequence from Plasmodium falciparum with , , , and as ligands. Active as Adenylosuccinate synthase, with EC number 6.3.4.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of fully ligated adenylosuccinate synthetase from Plasmodium falciparum., Eaazhisai K, Jayalakshmi R, Gayathri P, Anand RP, Sumathy K, Balaram H, Murthy MR, J Mol Biol. 2004 Jan 30;335(5):1251-64. PMID:14729341

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