Structural and computational analysis of peptide recognition mechanism of class-C type penicillin binding protein, alkaline D-peptidase from Bacillus cereus DF4-B-Reference-Cited by-同舟云学术

Structural and computational analysis of peptide recognition mechanism of class-C type penicillin binding protein, alkaline D-peptidase from Bacillus cereus DF4-B

Published:2015-09-15 Issue:1 Volume:5 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Nakano Shogo,Okazaki Seiji,Ishitsubo Erika,Kawahara Nobuhiro,Komeda Hidenobu,Tokiwa Hiroaki,Asano Yasuhisa

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep13836.pdf

Reference41 articles.

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2. Fisher, J. F., Meroueh, S. O. & Mobashery, S. Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity. Chem Rev 105, 395–424, 10.1021/cr030102i (2005).

3. Tipper, D. J. & Strominger, J. L. Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc Natl Acad Sci USA 54, 1133–1141 (1965).

4. Poole, K. Resistance to beta-lactam antibiotics. Cell Mol Life Sci 61, 2200–2223, 10.1007/s00018-004-4060-9 (2004).

5. Bompard-Gilles, C. et al. Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the ‘penicillin-recognizing enzyme’ family. Structure 8, 971–980 (2000).

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