TY - JOUR
T1 - Crystal structure of an EfPDF complex with Met-Ala-Ser based on crystallographic packing
AU - Nam, Ki Hyun
AU - Kim, Kook Han
AU - Kim, Eunice Eun Kyeong
AU - Hwang, Kwang Yeon
N1 - Funding Information:
We thank H.S. Lee, K.H. Kim and K.J. Kim for assistance during data collection at beamline 4A of the Pohang Light Source, Korea. This study was supported by the National R&D Program for Cancer Control from the Ministry of Health & Welfare (Grant numbers: 0720160). K.H. Nam was supported by the Brain Korea 21 program.
PY - 2009/4/17
Y1 - 2009/4/17
N2 - PDF (peptide deformylase) plays a critical role in the production of mature proteins by removing the N-formyl 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.
AB - PDF (peptide deformylase) plays a critical role in the production of mature proteins by removing the N-formyl 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.
KW - Antibacterial drug design
KW - EfPDF-MAS
KW - PDF
KW - Peptide deformylase
UR - http://www.scopus.com/inward/record.url?scp=62649139034&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2009.02.113
DO - 10.1016/j.bbrc.2009.02.113
M3 - Article
C2 - 19249287
AN - SCOPUS:62649139034
SN - 0006-291X
VL - 381
SP - 630
EP - 633
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -