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| {{STRUCTURE_1n5n| PDB=1n5n | SCENE= }} | | {{STRUCTURE_1n5n| PDB=1n5n | SCENE= }} |
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| '''Crystal Structure of Peptide Deformylase from Pseudomonas aeruginosa'''
| | ===Crystal Structure of Peptide Deformylase from Pseudomonas aeruginosa=== |
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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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12823970}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12823970 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12823970}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Drug design]] | | [[Category: Drug design]] |
| [[Category: Metalloenzyme]] | | [[Category: Metalloenzyme]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:07:26 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:02:19 2008'' |
