| RRC ID |
60653
|
| 著者 |
Lee KO, Kong M, Kim I, Bai J, Cha S, Kim B, Ryu KS, Ryu S, Suh JY.
|
| タイトル |
Structural Basis for Cell-Wall Recognition by Bacteriophage PBC5 Endolysin.
|
| ジャーナル |
Structure
|
| Abstract |
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 β 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 crosslink, implicating the tertiary structure of peptidoglycan as the recognition motif of endolysins.
|
| 巻・号 |
27(9)
|
| ページ |
1355-1365.e4
|
| 公開日 |
2019-9-3
|
| DOI |
10.1016/j.str.2019.07.001
|
| PII |
S0969-2126(19)30233-3
|
| PMID |
31353242
|
| MeSH |
Bacillus cereus / cytology
Bacillus cereus / metabolism
Bacillus cereus / virology*
Bacteriophages / metabolism
Bacteriophages / pathogenicity*
Binding Sites
Cell Wall / chemistry
Cell Wall / metabolism
Crystallography, X-Ray
Endopeptidases / chemistry*
Endopeptidases / metabolism*
Hydrolysis
Models, Molecular
Peptidoglycan / chemistry*
Peptidoglycan / metabolism*
Protein Domains
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
|
| IF |
4.576
|
| 引用数 |
1
|
| リソース情報 |
| 一般微生物 |
JCM2505 |
