2p6w: Difference between revisions

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==Overview==

Paramecium bursaria chlorella virus-1 encodes at least five putative, glycosyltransferases that are probably involved in the synthesis of the, glycan components of the viral major capsid protein. The 1.6 A crystal, structure of one of these glycosyltransferases (A64R) has a mixed, alpha/beta fold containing a central, six-stranded beta sheet flanked by, alpha helices. Crystal structures of A64R, complexed with UDP, CMP, or, GDP, established that only UDP bound to A64R in the presence of Mn(2+), consistent with its high structural similarity to glycosyltransferases, which utilize UDP as the sugar carrier. The structure of the complex of, A64R, UDP-glucose, and Mn(2+) showed that the largest conformational, change occurred when hydrogen bonds were formed with the ligands. Unlike, UDP-glucose, UDP-galactose and UDP-GlcNAc did not bind to A64R, suggesting, a selective binding of UDP-glucose. Thus, UDP-glucose is most likely the, sugar donor for A64R, consistent with glucose occurring in the virus major, capsid protein glycans.

Paramecium bursaria chlorella virus-1 encodes at least five putative glycosyltransferases that are probably involved in the synthesis of the glycan components of the viral major capsid protein. The 1.6 A crystal structure of one of these glycosyltransferases (A64R) has a mixed alpha/beta fold containing a central, six-stranded beta sheet flanked by alpha helices. Crystal structures of A64R, complexed with UDP, CMP, or GDP, established that only UDP bound to A64R in the presence of Mn(2+), consistent with its high structural similarity to glycosyltransferases which utilize UDP as the sugar carrier. The structure of the complex of A64R, UDP-glucose, and Mn(2+) showed that the largest conformational change occurred when hydrogen bonds were formed with the ligands. Unlike UDP-glucose, UDP-galactose and UDP-GlcNAc did not bind to A64R, suggesting a selective binding of UDP-glucose. Thus, UDP-glucose is most likely the sugar donor for A64R, consistent with glucose occurring in the virus major capsid protein glycans.

==About this Structure==

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[[Category: Paramecium bursaria chlorella virus 1]]

[[Category: Single protein]]

[[Category: Etten, J.L.Van.]]

[[Category: Etten, J L.Van.]]

[[Category: Rossmann, M.G.]]

[[Category: Rossmann, M G.]]

[[Category: Ye, X.]]

[[Category: Zhang, Y.]]

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[[Category: pbcv]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Paramecium bursaria chlorella virus-1 encodes at least five putative, glycosyltransferases that are probably involved in the synthesis of the, glycan components of the viral major capsid protein. The 1.6 A crystal, structure of one of these glycosyltransferases (A64R) has a mixed, alpha/beta fold containing a central, six-stranded beta sheet flanked by, alpha helices. Crystal structures of A64R, complexed with UDP, CMP, or, GDP, established that only UDP bound to A64R in the presence of Mn(2+), consistent with its high structural similarity to glycosyltransferases, which utilize UDP as the sugar carrier. The structure of the complex of, A64R, UDP-glucose, and Mn(2+) showed that the largest conformational, change occurred when hydrogen bonds were formed with the ligands. Unlike, UDP-glucose, UDP-galactose and UDP-GlcNAc did not bind to A64R, suggesting, a selective binding of UDP-glucose. Thus, UDP-glucose is most likely the, sugar donor for A64R, consistent with glucose occurring in the virus major, capsid protein glycans.
+Paramecium bursaria chlorella virus-1 encodes at least five putative glycosyltransferases that are probably involved in the synthesis of the glycan components of the viral major capsid protein. The 1.6 A crystal structure of one of these glycosyltransferases (A64R) has a mixed alpha/beta fold containing a central, six-stranded beta sheet flanked by alpha helices. Crystal structures of A64R, complexed with UDP, CMP, or GDP, established that only UDP bound to A64R in the presence of Mn(2+), consistent with its high structural similarity to glycosyltransferases which utilize UDP as the sugar carrier. The structure of the complex of A64R, UDP-glucose, and Mn(2+) showed that the largest conformational change occurred when hydrogen bonds were formed with the ligands. Unlike UDP-glucose, UDP-galactose and UDP-GlcNAc did not bind to A64R, suggesting a selective binding of UDP-glucose. Thus, UDP-glucose is most likely the sugar donor for A64R, consistent with glucose occurring in the virus major capsid protein glycans.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Paramecium bursaria chlorella virus 1]]
 [[Category: Single protein]]
-[[Category: Etten, J.L.Van.]]
+[[Category: Etten, J L.Van.]]
-[[Category: Rossmann, M.G.]]
+[[Category: Rossmann, M G.]]
 [[Category: Ye, X.]]
 [[Category: Zhang, Y.]]
@@ Line 23: / Line 23: @@
 [[Category: pbcv]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:49:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:26:28 2008''