2OKL

Crystal structure of Peptide Deformylase 2 with actinonin from Bacillus cereus

Summary for 2OKL

• Entry DOI: 10.2210/pdb2okl/pdb
• Related: 1WS0 1WS1
• Descriptor: Peptide deformylase 2, ZINC ION, ACTINONIN, ... (5 entities in total)
• Functional Keywords: hydrolase
• Biological source: Bacillus cereus
• Total number of polymer chains: 2
• Total formula weight: 43141.96

Authors

Kim, E.E. (deposition date: 2007-01-17, release date: 2008-01-15, Last modification date: 2023-12-27)

Primary citation

Park, J.K.,Kim, K.H.,Moon, J.H.,Kim, E.E.
Characterization of Peptide Deformylase2 from B. cereus
J.Biochem.Mol.Biol., 40:1050-1057, 2007

PubMed 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.

PubMed: 18047803

Experimental method

X-RAY DIFFRACTION (1.7 Å)