| http://purl.uniprot.org/citations/12823970 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12823970 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12823970 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0022-2836(03)00596-5"xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0022-2836(03)00596-5"xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Lesley S.A."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Lesley S.A."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Kreusch A."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Kreusch A."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Lee C.C."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Lee C.C."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "McMullan D."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "McMullan D."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Shin T."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Shin T."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Spraggon G."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Spraggon G."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Vincent J."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Vincent J."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Ng K."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Ng K."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Ericson C."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Ericson C."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Klock H."xsd:string |
| http://purl.uniprot.org/citations/12823970 | http://purl.uniprot.org/core/author | "Klock H."xsd:string |