1jym

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[[Image:1jym.gif|left|200px]]
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{{STRUCTURE_1jym| PDB=1jym | SCENE= }}
{{STRUCTURE_1jym| PDB=1jym | SCENE= }}
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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'''
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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===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12005434 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12005434}}
==About this Structure==
==About this Structure==
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[[Category: Pdf]]
[[Category: Pdf]]
[[Category: Plasmodium]]
[[Category: Plasmodium]]
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Revision as of 18:07, 1 July 2008

Template:STRUCTURE 1jym

Crystals of Peptide Deformylase from Plasmodium falciparum with Ten Subunits per Asymmetric Unit Reveal Critical Characteristics of the Active Site for Drug Design

Template:ABSTRACT PUBMED 12005434

About this Structure

1JYM is a Single protein structure of sequence from Plasmodium falciparum. 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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