1lme

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[[Image:1lme.gif|left|200px]]
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{{STRUCTURE_1lme| PDB=1lme | SCENE= }}
{{STRUCTURE_1lme| PDB=1lme | SCENE= }}
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'''Crystal Structure of Peptide Deformylase from Thermotoga maritima'''
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===Crystal Structure of Peptide Deformylase from Thermotoga maritima===
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==Overview==
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Peptide deformylase (PDF) has received considerable attention during the last few years as a potential target for a new type of antibiotics. It is an essential enzyme in eubacteria for the removal of the formyl group from the N terminus of the nascent polypeptide chain. We have solved the X-ray structures of four members of this enzyme family, two from the Gram-positive pathogens Streptococcus pneumoniae and Staphylococcus aureus, and two from the Gram-negative bacteria Thermotoga maritima and Pseudomonas aeruginosa. Combined with the known structures from the Escherichia coli enzyme and the recently solved structure of the eukaryotic deformylase from Plasmodium falciparum, a complete picture of the peptide deformylase structure and function relationship is emerging. This understanding could help guide a more rational design of inhibitors. A structure-based comparison between PDFs reveals some conserved differences between type I and type II enzymes. Moreover, our structures provide insights into the known instability of PDF caused by oxidation of the metal-ligating cysteine residue.
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(as it appears on PubMed at http://www.pubmed.gov), where 12823970 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12823970}}
==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Thermophile]]
[[Category: Thermophile]]
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Revision as of 18:25, 2 July 2008

Image:1lme.png

Template:STRUCTURE 1lme

Crystal Structure of Peptide Deformylase from Thermotoga maritima

Template:ABSTRACT PUBMED 12823970

About this Structure

1LME is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Structure analysis of peptide deformylases from Streptococcus pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase., Kreusch A, Spraggon G, Lee CC, Klock H, McMullan D, Ng K, Shin T, Vincent J, Warner I, Ericson C, Lesley SA, J Mol Biol. 2003 Jul 4;330(2):309-21. PMID:12823970

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