2bsd: Difference between revisions

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==Overview==

Lactococcus lactis is a Gram-positive bacterium used extensively by the, dairy industry for the manufacture of fermented milk products. The, double-stranded DNA bacteriophage p2 infects specific L. lactis strains, using a receptor-binding protein (RBP) located at the tip of its, noncontractile tail. We have solved the crystal structure of phage p2 RBP, a homotrimeric protein composed of three domains: the shoulders, a, beta-sandwich attached to the phage; the neck, an interlaced beta-prism;, and the receptor-recognition head, a seven-stranded beta-barrel. We used, the complex of RBP with a neutralizing llama VHH domain to identify the, receptor-binding site. Structural similarity between the recognition-head, domain of phage p2 and those of adenoviruses and reoviruses, which invade, mammalian cells, suggests that these viruses, despite evolutionary distant, targets, lack of sequence similarity and the different chemical nature of, their genomes (DNA versus RNA), might have a common ancestral gene.

Lactococcus lactis is a Gram-positive bacterium used extensively by the dairy industry for the manufacture of fermented milk products. The double-stranded DNA bacteriophage p2 infects specific L. lactis strains using a receptor-binding protein (RBP) located at the tip of its noncontractile tail. We have solved the crystal structure of phage p2 RBP, a homotrimeric protein composed of three domains: the shoulders, a beta-sandwich attached to the phage; the neck, an interlaced beta-prism; and the receptor-recognition head, a seven-stranded beta-barrel. We used the complex of RBP with a neutralizing llama VHH domain to identify the receptor-binding site. Structural similarity between the recognition-head domain of phage p2 and those of adenoviruses and reoviruses, which invade mammalian cells, suggests that these viruses, despite evolutionary distant targets, lack of sequence similarity and the different chemical nature of their genomes (DNA versus RNA), might have a common ancestral gene.

==About this Structure==

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[[Category: Single protein]]

[[Category: Cambillau, C.]]

[[Category: Dehaard, H.J.W.]]

[[Category: Dehaard, H J.W.]]

[[Category: Desmyter, A.]]

[[Category: Moineau, S.]]

[[Category: Spinelli, S.]]

[[Category: Verrips, C.T.]]

[[Category: Verrips, C T.]]

[[Category: lactococcus lactis]]

[[Category: llama vhh]]

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[[Category: receptor binding protein]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Lactococcus lactis is a Gram-positive bacterium used extensively by the, dairy industry for the manufacture of fermented milk products. The, double-stranded DNA bacteriophage p2 infects specific L. lactis strains, using a receptor-binding protein (RBP) located at the tip of its, noncontractile tail. We have solved the crystal structure of phage p2 RBP, a homotrimeric protein composed of three domains: the shoulders, a, beta-sandwich attached to the phage; the neck, an interlaced beta-prism;, and the receptor-recognition head, a seven-stranded beta-barrel. We used, the complex of RBP with a neutralizing llama VHH domain to identify the, receptor-binding site. Structural similarity between the recognition-head, domain of phage p2 and those of adenoviruses and reoviruses, which invade, mammalian cells, suggests that these viruses, despite evolutionary distant, targets, lack of sequence similarity and the different chemical nature of, their genomes (DNA versus RNA), might have a common ancestral gene.
+Lactococcus lactis is a Gram-positive bacterium used extensively by the dairy industry for the manufacture of fermented milk products. The double-stranded DNA bacteriophage p2 infects specific L. lactis strains using a receptor-binding protein (RBP) located at the tip of its noncontractile tail. We have solved the crystal structure of phage p2 RBP, a homotrimeric protein composed of three domains: the shoulders, a beta-sandwich attached to the phage; the neck, an interlaced beta-prism; and the receptor-recognition head, a seven-stranded beta-barrel. We used the complex of RBP with a neutralizing llama VHH domain to identify the receptor-binding site. Structural similarity between the recognition-head domain of phage p2 and those of adenoviruses and reoviruses, which invade mammalian cells, suggests that these viruses, despite evolutionary distant targets, lack of sequence similarity and the different chemical nature of their genomes (DNA versus RNA), might have a common ancestral gene.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Cambillau, C.]]
-[[Category: Dehaard, H.J.W.]]
+[[Category: Dehaard, H J.W.]]
 [[Category: Desmyter, A.]]
 [[Category: Moineau, S.]]
 [[Category: Spinelli, S.]]
-[[Category: Verrips, C.T.]]
+[[Category: Verrips, C T.]]
 [[Category: lactococcus lactis]]
 [[Category: llama vhh]]
@@ Line 25: / Line 25: @@
 [[Category: receptor binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:29:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:08 2008''