Structural bases of peptidoglycan recognition by lysostaphin SH3b domain-Reference-Cited by-同舟云学术

Structural bases of peptidoglycan recognition by lysostaphin SH3b domain

Published:2019-04-12 Issue:1 Volume:9 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Mitkowski Paweł,Jagielska Elżbieta,Nowak Elżbieta,Bujnicki Janusz M.^ORCID,Stefaniak Filip^ORCID,Niedziałek Dorota,Bochtler Matthias^ORCID,Sabała Izabela

Funder

Fundacja na rzecz Nauki Polskiej

Ministry of Science and Higher Education | Narodowe Centrum Badań i Rozwoju

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41598-019-42435-z.pdf

Reference59 articles.

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2. Buist, G., Steen, A., Kok, J. & Kuipers, O. R. LysM, a widely distributed protein motif for binding to (peptido)glycans. Molecular microbiology 68, 838–847, https://doi.org/10.1111/j.1365-2958.2008.06211.x (2008).

3. Hermoso, J. A. et al. Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1. Structure 11, 1239–1249 (2003).

4. Donovan, D. M. & Foster-Frey, J. LambdaSa2 prophage endolysin requires Cpl-7-binding domains and amidase-5 domain for antimicrobial lysis of streptococci. FEMS microbiology letters 287, 22–33, https://doi.org/10.1111/j.1574-6968.2008.01287.x (2008).

5. Becker, S. C., Foster-Frey, J., Stodola, A. J., Anacker, D. & Donovan, D. M. Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain. Gene 443, 32–41, https://doi.org/10.1016/j.gene.2009.04.023 (2009).

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