期刊
STRUCTURE
卷 27, 期 9, 页码 1355-+出版社
CELL PRESS
DOI: 10.1016/j.str.2019.07.001
关键词
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资金
- Creative-Pioneering Researchers Program through Seoul National University [500-20170161]
- National Research Foundation of Korea [NRF-2017R1A2B4004471, 2016R1A2B4015436, NRF-2017R1A2A1A17069378]
- KBSI grant [T39632]
- BK21 Plus Program of the Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea
- National Research Foundation of Korea [2016R1A2B4015436] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Phage endolysins are hydrolytic enzymes that cleave the bacterial cell wall during the lytic cycle. We isolated the bacteriophage PBC5 against Bacillus cereus, a major foodborne pathogen, and describe the molecular interaction between endolysin LysPBC5 and the host peptidoglycan structure. LysPBC5 has an N-terminal glycoside hydrolase 25 domain, and a C-terminal cell-wall binding domain (CBD) that is critical for specific cell-wall recognition and lysis. The crystal and solution structures of CBDs reveal tandem SH3b domains that are tightly engaged with each other. The CBD binds to the peptidoglycan in a bidentate manner via distal beta sheet motifs with pseudo 2-fold symmetry, which can explain its high affinity and host specificity. The CBD primarily interacts with the glycan strand of the peptidoglycan layer instead of the peptide cross-link, implicating the tertiary structure of peptidoglycan as the recognition motif of endolysins.
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