Crystal structure of an EfPDF complex with Met-Ala-Ser based on crystallographic packing

Title
Crystal structure of an EfPDF complex with Met-Ala-Ser based on crystallographic packing
Authors
남기현김국한김은경황광연
Keywords
PDF; Peptide deformylase; EfPDF-MAS; Antibacterial drug design
Issue Date
2009-04
Publisher
Biochemical and biophysical research communications
Citation
VOL 381, 630-633
Abstract
PDF (peptide deformylase) plays a critical role in the production of mature proteins by removing the Nformyl polypeptide of nascent proteins in the prokaryote cell system. This protein is essential for bacterial growth, making it an attractive target for the design of new antibiotics. Accordingly, PDF has been evaluated as a drug target; however, architectural mechanism studies of PDF have not yet fully elucidated its molecular function. We recently reported the crystal structure of PDF produced by Enterococcus faecium [K.H. Nam, J.I. Ham, A. Priyadarshi, E.E. Kim, N. Chung, K.Y. Hwang, ‘‘Insight into the antibacterial drug design and architectural mechanism of peptide recognition from the E. faecium peptide deformylase structure”, Proteins 74 (2009) 261–265]. Here, we present the crystal structure of the EfPDF complex with MAS (Met-Ser-Ala), thereby not only delineating the architectural mechanism for the recognition of mimic-peptides by N-terminal cleaved expression peptide, but also suggesting possible targets for rational design of antibacterial drugs. In addition to their implications for drug design, these structural studies will facilitate elucidation of the architectural mechanism responsible for the peptide recognition of PDF.
URI
http://pubs.kist.re.kr/handle/201004/35680
ISSN
1090-2104
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