Structural and biochemical characterizations of the novel autolysin Acd24020 from Clostridioides difficile and its full‐function catalytic domain as a lytic enzyme-Reference-Cited by-同舟云学术

Structural and biochemical characterizations of the novel autolysin Acd24020 from Clostridioides difficile and its full‐function catalytic domain as a lytic enzyme

Published:2020-11-22 Issue:4 Volume:115 Page:684-698
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Mol. Microbiol.

Author:

Sekiya Hiroshi¹,Tamai Eiji¹²^ORCID,Kawasaki Jurina¹,Murakami Kaho¹,Kamitori Shigehiro²^ORCID

Affiliation:

1. Department of Infectious Disease College of Pharmaceutical Science Matsuyama University Matsuyama Japan

2. Life Science Research Center and Faculty of Medicine Kagawa University Miki‐cho, Kita‐gun Japan

Funder

Japan Society for the Promotion of Science

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/mmi.14636

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2. RipD (Rv1566c) from Mycobacterium tuberculosis: adaptation of an NlpC/p60 domain to a non-catalytic peptidoglycan-binding function

3. Catalytic diversity and cell wall binding repeats in the phage-encoded endolysins

4. Version 1.2 of the Crystallography and NMR system

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