1jym
From Proteopedia
(New page: 200px<br /><applet load="1jym" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jym, resolution 2.80Å" /> '''Crystals of Peptide ...) |
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| - | [[Image:1jym.gif|left|200px]]<br /><applet load="1jym" size=" | + | [[Image:1jym.gif|left|200px]]<br /><applet load="1jym" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jym, resolution 2.80Å" /> | caption="1jym, resolution 2.80Å" /> | ||
'''Crystals of Peptide Deformylase from Plasmodium falciparum with Ten Subunits per Asymmetric Unit Reveal Critical Characteristics of the Active Site for Drug Design'''<br /> | '''Crystals of Peptide Deformylase from Plasmodium falciparum with Ten Subunits per Asymmetric Unit Reveal Critical Characteristics of the Active Site for Drug Design'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Peptide deformylase catalyzes the deformylation reaction of the amino | + | Peptide deformylase catalyzes the deformylation reaction of the amino terminal fMet residue of newly synthesized proteins in bacteria, and most likely in Plasmodium falciparum, and has therefore been identified as a potential antibacterial and antimalarial drug target. The structure of P. falciparum peptide deformylase, determined at 2.8 A resolution with ten subunits per asymmetric unit, is similar to the bacterial enzyme with the residues involved in catalysis, the position of the bound metal ion, and a catalytically important water structurally conserved between the two enzymes. However, critical differences in the substrate binding region explain the poor affinity of E. coli deformylase inhibitors and substrates toward the Plasmodium enzyme. The Plasmodium structure serves as a guide for designing novel antimalarials. |
==About this Structure== | ==About this Structure== | ||
| - | 1JYM 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 CO as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] Full crystallographic information is available from [http:// | + | 1JYM 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=CO:'>CO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JYM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hirsh, I.]] | [[Category: Hirsh, I.]] | ||
| - | [[Category: Hol, W | + | [[Category: Hol, W G.J.]] |
[[Category: Kumar, A.]] | [[Category: Kumar, A.]] | ||
| - | [[Category: Nguyen, K | + | [[Category: Nguyen, K T.]] |
[[Category: Ornstein, B.]] | [[Category: Ornstein, B.]] | ||
[[Category: Pei, D.]] | [[Category: Pei, D.]] | ||
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[[Category: plasmodium]] | [[Category: plasmodium]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:12 2008'' |
Revision as of 11:28, 21 February 2008
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Crystals of Peptide Deformylase from Plasmodium falciparum with Ten Subunits per Asymmetric Unit Reveal Critical Characteristics of the Active Site for Drug Design
Overview
Peptide deformylase catalyzes the deformylation reaction of the amino terminal fMet residue of newly synthesized proteins in bacteria, and most likely in Plasmodium falciparum, and has therefore been identified as a potential antibacterial and antimalarial drug target. The structure of P. falciparum peptide deformylase, determined at 2.8 A resolution with ten subunits per asymmetric unit, is similar to the bacterial enzyme with the residues involved in catalysis, the position of the bound metal ion, and a catalytically important water structurally conserved between the two enzymes. However, critical differences in the substrate binding region explain the poor affinity of E. coli deformylase inhibitors and substrates toward the Plasmodium enzyme. The Plasmodium structure serves as a guide for designing novel antimalarials.
About this Structure
1JYM is a Single protein structure of sequence from Plasmodium falciparum with as ligand. Active as Formylmethionine deformylase, with EC number 3.5.1.31 Full crystallographic information is available from OCA.
Reference
Crystals of peptide deformylase from Plasmodium falciparum reveal critical characteristics of the active site for drug design., Kumar A, Nguyen KT, Srivathsan S, Ornstein B, Turley S, Hirsh I, Pei D, Hol WG, Structure. 2002 Mar;10(3):357-67. PMID:12005434
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