2bat: Difference between revisions

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[[Image:2bat.gif|left|200px]]<br /><applet load="2bat" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2bat.gif|left|200px]]<br /><applet load="2bat" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2bat, resolution 2.0Å" />

'''THE STRUCTURE OF THE COMPLEX BETWEEN INFLUENZA VIRUS NEURAMINIDASE AND SIALIC ACID, THE VIRAL RECEPTOR'''<br />

==Overview==

Crystallographic studies of neuraminidase-sialic acid complexes indicate, that sialic acid is distorted on binding the enzyme. Three arginine, residues on the enzyme interact with the carboxylate group of the sugar, which is observed to be equatorial to the saccharide ring as a consequence, of its distorted geometry. The glycosidic oxygen is positioned within, hydrogen-bonding distance of Asp-151, implicating this residue in, catalysis.

Crystallographic studies of neuraminidase-sialic acid complexes indicate that sialic acid is distorted on binding the enzyme. Three arginine residues on the enzyme interact with the carboxylate group of the sugar which is observed to be equatorial to the saccharide ring as a consequence of its distorted geometry. The glycosidic oxygen is positioned within hydrogen-bonding distance of Asp-151, implicating this residue in catalysis.

==About this Structure==

2BAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NAG, SIA and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2BAT OCA].

2BAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=SIA:'>SIA</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BAT OCA].

==Reference==

Line 13:

[[Category: Exo-alpha-sialidase]]

[[Category: Single protein]]

[[Category: Colman, P.M.]]

[[Category: Colman, P M.]]

[[Category: Varghese, J.N.]]

[[Category: Varghese, J N.]]

[[Category: CA]]

[[Category: NAG]]

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[[Category: hydrolase(o-glycosyl)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 08:41:~~02 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:47 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2bat.gif|left|200px]]<br /><applet load="2bat" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2bat.gif|left|200px]]<br /><applet load="2bat" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2bat, resolution 2.0&Aring;" />
 '''THE STRUCTURE OF THE COMPLEX BETWEEN INFLUENZA VIRUS NEURAMINIDASE AND SIALIC ACID, THE VIRAL RECEPTOR'''<br />
 ==Overview==
-Crystallographic studies of neuraminidase-sialic acid complexes indicate, that sialic acid is distorted on binding the enzyme. Three arginine, residues on the enzyme interact with the carboxylate group of the sugar, which is observed to be equatorial to the saccharide ring as a consequence, of its distorted geometry. The glycosidic oxygen is positioned within, hydrogen-bonding distance of Asp-151, implicating this residue in, catalysis.
+Crystallographic studies of neuraminidase-sialic acid complexes indicate that sialic acid is distorted on binding the enzyme. Three arginine residues on the enzyme interact with the carboxylate group of the sugar which is observed to be equatorial to the saccharide ring as a consequence of its distorted geometry. The glycosidic oxygen is positioned within hydrogen-bonding distance of Asp-151, implicating this residue in catalysis.
 ==About this Structure==
-BAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NAG, SIA and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BAT OCA].
+BAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=SIA:'>SIA</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BAT OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Exo-alpha-sialidase]]
 [[Category: Single protein]]
-[[Category: Colman, P.M.]]
+[[Category: Colman, P M.]]
-[[Category: Varghese, J.N.]]
+[[Category: Varghese, J N.]]
 [[Category: CA]]
 [[Category: NAG]]
@@ Line 20: / Line 20: @@
 [[Category: hydrolase(o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:41:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:47 2008''