1dff
From Proteopedia
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PEPTIDE DEFORMYLASE
Overview
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.
About this Structure
1DFF is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Active as Formylmethionine deformylase, with EC number 3.5.1.31 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of the Escherichia coli peptide deformylase., Chan MK, Gong W, Rajagopalan PT, Hao B, Tsai CM, Pei D, Biochemistry. 1997 Nov 11;36(45):13904-9. PMID:9374869
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