1dff: Difference between revisions
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[[Category: zinc metalloprotease]] | [[Category: zinc metalloprotease]] | ||
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Revision as of 15:56, 30 October 2007
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PEPTIDE DEFORMYLASE
OverviewOverview
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. ... [(full description)]
About this StructureAbout 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]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
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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