Structure and chemistry of lysinoalanine crosslinking in the spirochaete flagella hook
Author:
Funder
U.S. Department of Health and Human Services
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/s41589-019-0341-3.pdf
Reference57 articles.
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2. Walden, M., Crow, A., Nelson, M. D. & Banfield, M. J. Intramolecular isopeptide but not internal thioester bonds confer proteolytic and significant thermal stability to the S. pyogenes pilus adhesin Spy0125. Proteins Struct. Funct. Bioinforma. 82, 517–527 (2014).
3. Kwon, H. et al. Autocatalytically generated Thr-Gln ester bond crosslinks stabilize the repetitive Ig-domain shaft of a bacterial cell surface adhesin. PNAS 111, 1367–1372 (2014).
4. Baker, E. N., Squire, C. J. & Young, P. G. Self-generated covalent crosslinks in the cell-surface adhesins of Gram-positive bacteria. Biochem. Soc. Trans. 43, 787–794 (2015).
5. Popa, M. P., McKelvey, T. A., Hempel, J. & Hendrix, R. W. Bacteriophage HK97 structure: wholesale covalent crosslinking between the major head shell subunits. J. Virol. 65, 3227–3237 (1991).
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