Characterization of peptide deformylase2 from B. cereus.
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.
Life Sciences Division, Korea Institute of Science and Technology, 39-1 Hawolkok-dong, Sungbuk-gu, Seoul 136-791, Korea.
Joon Kyu
JK
Park
Kook-Han
KH
Kim
Jin Ho
JH
Moon
Eunice Eunkyeong
EE
Kim
D000581:Amidohydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D001409:Bacillus cereus / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D017931:DNA Primers / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D019281:Dimerization; D005798:Genes, Bacterial; D006877:Hydroxamic Acids / Q000737:chemistry; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity
D017931:DNA Primers; D004269:DNA, Bacterial; D006877:Hydroxamic Acids; D007527:Isoenzymes; D000581:Amidohydrolases; C084507:peptide deformylase; C010531:actinonin