2nw0: Difference between revisions

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==Overview==

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.

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.

==About this Structure==

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[[Category: Protein complex]]

[[Category: Unidentified phage]]

[[Category: Buckle, A.M.]]

[[Category: Buckle, A M.]]

[[Category: Porter, C.J.]]

[[Category: Porter, C J.]]

[[Category: Whisstock, J.C.]]

[[Category: Whisstock, J C.]]

[[Category: ACT]]

[[Category: beta barrel]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:12:02 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Protein complex]]
 [[Category: Unidentified phage]]
-[[Category: Buckle, A.M.]]
+[[Category: Buckle, A M.]]
-[[Category: Porter, C.J.]]
+[[Category: Porter, C J.]]
-[[Category: Whisstock, J.C.]]
+[[Category: Whisstock, J C.]]
 [[Category: ACT]]
 [[Category: beta barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:00:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:12:02 2008''