Park, Joon Kyu Kim, Kook-Han Moon, An Ho Kim, Eunice EunKyeong 2024-01-21T00:04:52Z 2024-01-21T00:04:52Z 2021-09-02 2007-11-30 1225-8687 https://pubs.kist.re.kr/handle/201004/133969 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. English SPRINGER SINGAPORE PTE LTD BACTERIUM LEPTOSPIRA-INTERROGANS STAPHYLOCOCCUS-AUREUS ANTIBACTERIAL AGENTS STREPTOCOCCUS-PNEUMONIAE CRYSTAL-STRUCTURE IN-VITRO INHIBITORS PROTEIN ACTINONIN DEHYDROGENASE Characterization of peptide deformylase2 from B-cereus Article 1 JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.40, no.6, pp.1050 - 1057 JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY 40 6 1050 1057 scie scopus kci ART001067291 000251141900027 2-s2.0-36949033891 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article BACTERIUM LEPTOSPIRA-INTERROGANS STAPHYLOCOCCUS-AUREUS ANTIBACTERIAL AGENTS STREPTOCOCCUS-PNEUMONIAE CRYSTAL-STRUCTURE IN-VITRO INHIBITORS PROTEIN ACTINONIN DEHYDROGENASE actinonin complex Bacillus cereus crystal structure peptide deformylase