| http://purl.uniprot.org/citations/9374869 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9374869 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9374869 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/9374869 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein synthesis in bacteria involves the formylation and deformylation of the N-terminal methionine. As eukaryotic organisms differ in their protein biosynthetic mechanisms, peptide deformylase, the bacterial enzyme responsible for deformylation, represents a potential target for antibiotic studies. Here we report the crystallization and 2.9 A X-ray structure solution of the zinc containing Escherichia coli peptide deformylase. While the primary sequence, tertiary structure, and use of coordinated cysteine suggest that E. coli deformylase belongs to a new subfamily of metalloproteases, the environment around the metal appears to have strong geometric similarity to the active sites of the thermolysin family. This suggests a possible similarity in their hydrolytic mechanisms. Another important issue is the origin of the enzyme's specificity for N-formylated over N-acetylated substrates. Based on the structure, the specificity appears to result from hydrogen-bonding interactions which orient the substrate for cleavage, and steric factors which physically limit the size of the N-terminal carbonyl group."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi9711543"xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi9711543"xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Gong W."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Gong W."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Hao B."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Hao B."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Pei D."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Pei D."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Chan M.K."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Chan M.K."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Rajagopalan P.T.R."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Rajagopalan P.T.R."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Tsai C.M."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/author | "Tsai C.M."xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/pages | "13904-13909"xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/pages | "13904-13909"xsd:string |
| http://purl.uniprot.org/citations/9374869 | http://purl.uniprot.org/core/title | "Crystal structure of the Escherichia coli peptide deformylase."xsd:string |