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KMID : 0380220070400061050
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Journal of Biochemistry and Molecular Biology
2007 Volume.40 No. 6 p.1050 ~ p.1057
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Characterization of Peptide Deformylase2 from B. cereus
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Park Joon-Kyu
Kim Kook-Han
Moon Jin-Ho
Kim Eunice EunKyeong
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Abstract
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Peptide deformylase (PDF) is a metalloenzyme that removes the N-terminal formyl groups from newly synthesized proteins. It is essential for bacterial survival, and is therefore-considered as a potential target for antimicrobial chemotherapy. However, some bacteria including medically relevant pathogens possess two or more def-like enes. Here we have examined two PDFs from Bacillus cereus. The two share only 32% sequence identity and the crystal structures show overall similarity with PDF2 having a longer C-terminus. However, there are differences at the two active sites, and these differences appear to contribute to the activity difference seen between the two. cPDF2 is found as a dimer in the crystal form with two additional actinonin bound at that interface.
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KEYWORD
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Actinonin complex, Bacillus cereus, Crystal structure, Peptide deformylase
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