1qwn: Difference between revisions

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

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

caption="1qwn, resolution 1.20Å" />

'''GOLGI ALPHA-MANNOSIDASE II Covalent Intermediate Complex with 5-fluoro-gulosyl-fluoride'''<br />

==Overview==

The family 38 golgi alpha-mannosidase II, thought to cleave mannosidic, bonds through a double displacement mechanism involving a reaction, intermediate, is a clinically important enzyme involved in glycoprotein, processing. The structure of three different covalent glycosyl-enzyme, intermediates have been determined to 1.2-A resolution for the Golgi, alpha-mannosidase II from Drosophila melanogaster by use of fluorinated, sugar analogues, both with the wild-type enzyme and a mutant enzyme in, which the acid/base catalyst has been removed. All these structures reveal, sugar intermediates bound in a distorted 1S5 skew boat conformation. The, similarity of this conformation with that of the substrate in the recently, determined structure of the Michaelis complex of a beta-mannanase (Ducros, V. M. A., Zechel, D. L., Murshudov, G. N., Gilbert, H. J., Szabo, L., Stoll, D., Withers, S. G., and Davies, G. J. (2002) Angew. Chem. Int. Ed., Engl. 41, 2824-2827) suggests that these disparate enzymes have recruited, common stereoelectronic features in evolving their catalytic mechanisms.

The family 38 golgi alpha-mannosidase II, thought to cleave mannosidic bonds through a double displacement mechanism involving a reaction intermediate, is a clinically important enzyme involved in glycoprotein processing. The structure of three different covalent glycosyl-enzyme intermediates have been determined to 1.2-A resolution for the Golgi alpha-mannosidase II from Drosophila melanogaster by use of fluorinated sugar analogues, both with the wild-type enzyme and a mutant enzyme in which the acid/base catalyst has been removed. All these structures reveal sugar intermediates bound in a distorted 1S5 skew boat conformation. The similarity of this conformation with that of the substrate in the recently determined structure of the Michaelis complex of a beta-mannanase (Ducros, V. M. A., Zechel, D. L., Murshudov, G. N., Gilbert, H. J., Szabo, L., Stoll, D., Withers, S. G., and Davies, G. J. (2002) Angew. Chem. Int. Ed. Engl. 41, 2824-2827) suggests that these disparate enzymes have recruited common stereoelectronic features in evolving their catalytic mechanisms.

==About this Structure==

1QWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with NAG, ZN, GUL, TRS and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,3-1,6-alpha-mannosidase Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.114 3.2.1.114] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1QWN OCA].

1QWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=GUL:'>GUL</scene>, <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,3-1,6-alpha-mannosidase Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.114 3.2.1.114] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWN OCA].

==Reference==

Line 14:

[[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]]

[[Category: Single protein]]

[[Category: Kuntz, D.A.]]

[[Category: Kuntz, D A.]]

[[Category: Numao, S.]]

[[Category: Rose, D.R.]]

[[Category: Rose, D R.]]

[[Category: Withers, S.G.]]

[[Category: Withers, S G.]]

[[Category: GUL]]

[[Category: MPD]]

Line 28:

[[Category: three helix bundle]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:28 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1qwn.gif|left|200px]]<br /><applet load="1qwn" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1qwn.gif|left|200px]]<br /><applet load="1qwn" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1qwn, resolution 1.20&Aring;" />
 '''GOLGI ALPHA-MANNOSIDASE II Covalent Intermediate Complex with 5-fluoro-gulosyl-fluoride'''<br />
 ==Overview==
-The family 38 golgi alpha-mannosidase II, thought to cleave mannosidic, bonds through a double displacement mechanism involving a reaction, intermediate, is a clinically important enzyme involved in glycoprotein, processing. The structure of three different covalent glycosyl-enzyme, intermediates have been determined to 1.2-A resolution for the Golgi, alpha-mannosidase II from Drosophila melanogaster by use of fluorinated, sugar analogues, both with the wild-type enzyme and a mutant enzyme in, which the acid/base catalyst has been removed. All these structures reveal, sugar intermediates bound in a distorted 1S5 skew boat conformation. The, similarity of this conformation with that of the substrate in the recently, determined structure of the Michaelis complex of a beta-mannanase (Ducros, V. M. A., Zechel, D. L., Murshudov, G. N., Gilbert, H. J., Szabo, L., Stoll, D., Withers, S. G., and Davies, G. J. (2002) Angew. Chem. Int. Ed., Engl. 41, 2824-2827) suggests that these disparate enzymes have recruited, common stereoelectronic features in evolving their catalytic mechanisms.
+The family 38 golgi alpha-mannosidase II, thought to cleave mannosidic bonds through a double displacement mechanism involving a reaction intermediate, is a clinically important enzyme involved in glycoprotein processing. The structure of three different covalent glycosyl-enzyme intermediates have been determined to 1.2-A resolution for the Golgi alpha-mannosidase II from Drosophila melanogaster by use of fluorinated sugar analogues, both with the wild-type enzyme and a mutant enzyme in which the acid/base catalyst has been removed. All these structures reveal sugar intermediates bound in a distorted 1S5 skew boat conformation. The similarity of this conformation with that of the substrate in the recently determined structure of the Michaelis complex of a beta-mannanase (Ducros, V. M. A., Zechel, D. L., Murshudov, G. N., Gilbert, H. J., Szabo, L., Stoll, D., Withers, S. G., and Davies, G. J. (2002) Angew. Chem. Int. Ed. Engl. 41, 2824-2827) suggests that these disparate enzymes have recruited common stereoelectronic features in evolving their catalytic mechanisms.
 ==About this Structure==
-QWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with NAG, ZN, GUL, TRS and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,3-1,6-alpha-mannosidase Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.114 3.2.1.114] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QWN OCA].
+QWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=GUL:'>GUL</scene>, <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,3-1,6-alpha-mannosidase Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.114 3.2.1.114] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWN OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]]
 [[Category: Single protein]]
-[[Category: Kuntz, D.A.]]
+[[Category: Kuntz, D A.]]
 [[Category: Numao, S.]]
-[[Category: Rose, D.R.]]
+[[Category: Rose, D R.]]
-[[Category: Withers, S.G.]]
+[[Category: Withers, S G.]]
 [[Category: GUL]]
 [[Category: MPD]]
@@ Line 28: / Line 28: @@
 [[Category: three helix bundle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:04:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:28 2008''