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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Characterization of Peptide Deformylase2 from B. cereus

  • Park, Joon-Kyu (Life Sciences Division, Korea Institute of Science and Technology) ;
  • Kim, Kook-Han (Life Sciences Division, Korea Institute of Science and Technology) ;
  • Moon, Jin-Ho (Life Sciences Division, Korea Institute of Science and Technology) ;
  • Kim, Eunice Eun-Kyeong (Life Sciences Division, Korea Institute of Science and Technology)
  • Published : 2007.11.30
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Abstract

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 genes. 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. BcPDF2 is found as a dimer in the crystal form with two additional actinonin bound at that interface.

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References

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