1lm6

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spinqualitylabelsall models 1lm6, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Peptide Deformylase from Streptococcus pneumoniae

Overview

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.

About this Structure

1LM6 is a Single protein structure of sequence from Streptococcus pneumoniae with FE and GOL as ligands. Active as Peptide deformylase, with EC number 3.5.1.88 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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