6ILU

Endolysin LysPBC5 CBD

6ILU の概要

• エントリーDOI: 10.2210/pdb6ilu/pdb
• 分子名称: Lysin, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: cell-wall binding, endolysin, pbc5, sh3b, sugar binding protein
• 由来する生物種: Bacillus phage PBC5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32551.85

構造登録者

Suh, J.Y.,Ryu, K.S.,Ryu, S.,Lee, K.O.,Kong, M.S.,Bae, J.W.,Kim, I.T. (登録日: 2018-10-19, 公開日: 2019-07-31, 最終更新日: 2024-03-27)

主引用文献

Lee, K.O.,Kong, M.,Kim, I.,Bai, J.,Cha, S.,Kim, B.,Ryu, K.S.,Ryu, S.,Suh, J.Y.
Structural Basis for Cell-Wall Recognition by Bacteriophage PBC5 Endolysin.
Structure, 27:1355-1365.e4, 2019

PubMed 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.

PubMed: 31353242
DOI: 10.1016/j.str.2019.07.001

実験手法

X-RAY DIFFRACTION (1.601 Å)