2fsd: Difference between revisions

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==Overview==

Lactococcus lactis, a gram-positive bacterium widely used by the dairy, industry, is subject to lytic phage infections. In the first step of, infection, phages recognize the host saccharidic receptor using their, receptor binding protein (RBP). Here, we report the 2.30-A-resolution, crystal structure of the RBP head domain from phage bIL170. The structure, of the head monomer is remarkably close to those of other lactococcal, phages, p2 and TP901-1, despite any sequence identity with them. The, knowledge of the three-dimensional structures of three RBPs gives a better, insight into the module exchanges which have occurred among phages.

Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry, is subject to lytic phage infections. In the first step of infection, phages recognize the host saccharidic receptor using their receptor binding protein (RBP). Here, we report the 2.30-A-resolution crystal structure of the RBP head domain from phage bIL170. The structure of the head monomer is remarkably close to those of other lactococcal phages, p2 and TP901-1, despite any sequence identity with them. The knowledge of the three-dimensional structures of three RBPs gives a better insight into the module exchanges which have occurred among phages.

==About this Structure==

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[[Category: receptor binding protein]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Lactococcus lactis, a gram-positive bacterium widely used by the dairy, industry, is subject to lytic phage infections. In the first step of, infection, phages recognize the host saccharidic receptor using their, receptor binding protein (RBP). Here, we report the 2.30-A-resolution, crystal structure of the RBP head domain from phage bIL170. The structure, of the head monomer is remarkably close to those of other lactococcal, phages, p2 and TP901-1, despite any sequence identity with them. The, knowledge of the three-dimensional structures of three RBPs gives a better, insight into the module exchanges which have occurred among phages.
+Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry, is subject to lytic phage infections. In the first step of infection, phages recognize the host saccharidic receptor using their receptor binding protein (RBP). Here, we report the 2.30-A-resolution crystal structure of the RBP head domain from phage bIL170. The structure of the head monomer is remarkably close to those of other lactococcal phages, p2 and TP901-1, despite any sequence identity with them. The knowledge of the three-dimensional structures of three RBPs gives a better insight into the module exchanges which have occurred among phages.
 ==About this Structure==
@@ Line 20: / Line 20: @@
 [[Category: receptor binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:43:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:38 2008''