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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2019.1
- 수록면
- 79 - 86 (8page)
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Endolysins are bacteriophage-derived enzymes that hydrolyze the peptidoglycan of host bacteria. Endolysins are considered to be promising tools for the control of pathogenic bacteria. LysB4 is an endolysin produced by Bacillus cereus-infecting bacteriophage B4, and consists of an N-terminal enzymatic active domain (EAD) and a C-terminal cell wall binding domain (CBD). LysB4 was discovered for the first time as an Lalanoyl-D-glutamate endopeptidase with the ability to breakdown the peptidoglycan among B. cereus-infecting phages. To understand the activity of LysB4 at the molecular level, this study determined the X-ray crystal structure of the LysB4 EAD, using the full-length LysB4 endolysin. The LysB4 EAD has an active site that is typical of LAS-type enzymes, where Zn2+ is tetrahedrally coordinated by three amino acid residues and one water molecule. Mutational studies identified essential residues that are involved in lytic activity. Based on the structural and biochemical information about LysB4, we suggest a ligand-docking model and a putative endopeptidase mechanism for the LysB4 EAD. These suggestions add insight into the molecular mechanism of the endolysin LysB4 in B. cereusinfecting phages.
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참고문헌 (31)
참고문헌 신청
Adams, P. D. / 2010 / PHENIX : a comprehensive Python-based system for macromolecular structure solution / Acta Crystallogr. D. Biol. Crystallogr 66:213~221
Asensio, J. L. / 2013 / Carbohydrate-aromatic interactions / Acc. Chem. Res 46:946~954
Bochtler, M. / 2004 / Similar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases / Protein Sci 13:854~861
Borysowski, J. / 2006 / Bacteriophage endolysins as a novel class of antibacterial agents / Exp. Biol. Med 231:366~377
Bussiere, D. E. / 1998 / The structure of VanX reveals a novel aminodipeptidase involved in mediating transposon-based vancomycin resistance / Mol. Cell 2:75~84
Asensio, J. L. / 2013 / Carbohydrate-aromatic interactions / Acc. Chem. Res 46:946~954
Bochtler, M. / 2004 / Similar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases / Protein Sci 13:854~861
Borysowski, J. / 2006 / Bacteriophage endolysins as a novel class of antibacterial agents / Exp. Biol. Med 231:366~377
Bussiere, D. E. / 1998 / The structure of VanX reveals a novel aminodipeptidase involved in mediating transposon-based vancomycin resistance / Mol. Cell 2:75~84
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