The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis.

The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis. Research Abstract Details 

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The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis. Abstract Text:

Corrine J Porter,Raymond Schuch,Adam J Pelzek,Ashley M Buckle,Sheena McGowan,Matthew C J Wilce,Jamie Rossjohn,Ryann Russell,Daniel Nelson,Vincent A Fischetti,James C Whisstock,

Lysins are peptidoglycan hydrolases that are produced by bacteriophage and act to lyse the bacterial host cell wall during progeny phage release. Here, we describe the structure and function of a novel bacteriophage-derived lysin, PlyB, which displays potent lytic activity against the Bacillus anthracis-like strain ATCC 4342. This molecule comprises an N-terminal catalytic domain (PlyB(cat)) and a C-terminal bacterial SH3-like domain, SH3b. It is shown that both domains are required for effective catalytic activity against ATCC 4342. Further, PlyB has specific activity comparable to the phage lysin PlyG, an amidase being developed as a therapeutic against anthrax. In contrast to PlyG, however, the 1.6 A X-ray crystal structure of PlyB(cat) reveals that the catalytic domain adopts the glycosyl hydrolase (GH)-25, rather than phage T7 lysozyme-like fold. PlyB therefore represents a new class of anthrax lysin and a new defensive tool in the armament against anthrax-mediated bioterrorism.

The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis. Publishing Authors By Initials

CJ Porter,R Schuch,AJ Pelzek,AM Buckle,S McGowan,MC Wilce,J Rossjohn,R Russell,D Nelson,VA Fischetti,JC Whisstock,

For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

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The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of molecular biology

VOLUME: 366

Page Numbers: 540-50

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 18

MONTH: 11

YEAR: 2006

The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis. Information

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LANGUAGE: eng

NlmUniqueID: 2985088

The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis. Keywords Mesh Terms:

KEYWORDS: Viral Proteins

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis. Information

Substance Name: PlyB bacteriophage lysin

Registry Number: EC 3.2.2.-

Grant and Affiliation Information for The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis.

AFFILIATION: Protein Crystallography Unit, Department of Biochemistry and Molecular Biology and The ARC Centre of Excellence for Structural and Functional Microbial Genomics, Monash University, Clayton, Melbourne, VIC 3800, Australia.

Country: England

AGENCY: United States NIAID

GRANT: AI057472

ACRONYM: AI

MEDLINETA: J Mol Biol

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ACCESSION NUMBER: 2NW0

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