PMID:9374869
| Citation |
Chan, MK, Gong, W, Rajagopalan, PT, Hao, B, Tsai, CM and Pei, D (1997) Crystal structure of the Escherichia coli peptide deformylase. Biochemistry 36:13904-9 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1021/bi9711543 |
| Keywords |
Amidohydrolases; Aminopeptidases/chemistry; Aminopeptidases/isolation & purification; Aminopeptidases/metabolism; Binding Sites; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Magnetic Resonance Spectroscopy; Metalloproteins/chemistry; Metalloproteins/isolation & purification; Metalloproteins/metabolism; Molecular Sequence Data; Protein Structure, Secondary; Protein Structure, Tertiary; Substrate Specificity; Thermolysin/chemistry; Zinc/metabolism |
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