1tyw: Difference between revisions

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[[Image:1tyw.gif|left|200px]]<br /><applet load="1tyw" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1tyw.gif|left|200px]]<br /><applet load="1tyw" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1tyw, resolution 1.8Å" />

'''STRUCTURE OF TAILSPIKE-PROTEIN'''<br />

==Overview==

The O-antigenic repeating units of lipopolysaccharides from Salmonella, serogroups A, B, and D1 serve as receptors for the phage P22 tailspike, protein, which also has receptor destroying endoglycosidase, (endorhamnosidase) activity, integrating the functions of both, hemagglutinin and neuraminidase in influenza virus. Crystal structures of, the tailspike protein in complex with oligosaccharides, comprising two, O-antigenic repeating units from Salmonella typhimurium, Salmonella, enteritidis, and Salmonella typhi 253Ty were determined at 1.8 A, resolution. The active-site topology with Asp-392, Asp-395, and Glu-359 as, catalytic residues was identified. Kinetics of binding and cleavage, suggest a role of the receptor destroying endorhamnosidase activity, primarily for detachment of newly assembled phages.

The O-antigenic repeating units of lipopolysaccharides from Salmonella serogroups A, B, and D1 serve as receptors for the phage P22 tailspike protein, which also has receptor destroying endoglycosidase (endorhamnosidase) activity, integrating the functions of both hemagglutinin and neuraminidase in influenza virus. Crystal structures of the tailspike protein in complex with oligosaccharides, comprising two O-antigenic repeating units from Salmonella typhimurium, Salmonella enteritidis, and Salmonella typhi 253Ty were determined at 1.8 A resolution. The active-site topology with Asp-392, Asp-395, and Glu-359 as catalytic residues was identified. Kinetics of binding and cleavage suggest a role of the receptor destroying endorhamnosidase activity primarily for detachment of newly assembled phages.

==About this Structure==

1TYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium_phage_p22 Salmonella typhimurium phage p22]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1TYW OCA].

1TYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium_phage_p22 Salmonella typhimurium phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYW OCA].

==Reference==

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[[Category: viral adhesion protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 03:42:~~30 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:47 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1tyw.gif|left|200px]]<br /><applet load="1tyw" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1tyw.gif|left|200px]]<br /><applet load="1tyw" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1tyw, resolution 1.8&Aring;" />
 '''STRUCTURE OF TAILSPIKE-PROTEIN'''<br />
 ==Overview==
-The O-antigenic repeating units of lipopolysaccharides from Salmonella, serogroups A, B, and D1 serve as receptors for the phage P22 tailspike, protein, which also has receptor destroying endoglycosidase, (endorhamnosidase) activity, integrating the functions of both, hemagglutinin and neuraminidase in influenza virus. Crystal structures of, the tailspike protein in complex with oligosaccharides, comprising two, O-antigenic repeating units from Salmonella typhimurium, Salmonella, enteritidis, and Salmonella typhi 253Ty were determined at 1.8 A, resolution. The active-site topology with Asp-392, Asp-395, and Glu-359 as, catalytic residues was identified. Kinetics of binding and cleavage, suggest a role of the receptor destroying endorhamnosidase activity, primarily for detachment of newly assembled phages.
+The O-antigenic repeating units of lipopolysaccharides from Salmonella serogroups A, B, and D1 serve as receptors for the phage P22 tailspike protein, which also has receptor destroying endoglycosidase (endorhamnosidase) activity, integrating the functions of both hemagglutinin and neuraminidase in influenza virus. Crystal structures of the tailspike protein in complex with oligosaccharides, comprising two O-antigenic repeating units from Salmonella typhimurium, Salmonella enteritidis, and Salmonella typhi 253Ty were determined at 1.8 A resolution. The active-site topology with Asp-392, Asp-395, and Glu-359 as catalytic residues was identified. Kinetics of binding and cleavage suggest a role of the receptor destroying endorhamnosidase activity primarily for detachment of newly assembled phages.
 ==About this Structure==
-TYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium_phage_p22 Salmonella typhimurium phage p22]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TYW OCA].
+TYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium_phage_p22 Salmonella typhimurium phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYW OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: viral adhesion protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:42:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:47 2008''