1qx1
From Proteopedia
(New page: 200px<br /><applet load="1qx1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qx1, resolution 1.30Å" /> '''Golgi alpha-mannosid...) |
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| - | [[Image:1qx1.jpg|left|200px]]<br /><applet load="1qx1" size=" | + | [[Image:1qx1.jpg|left|200px]]<br /><applet load="1qx1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qx1, resolution 1.30Å" /> | caption="1qx1, resolution 1.30Å" /> | ||
'''Golgi alpha-mannosidase II D341N mutant complex with 2-F-mannosyl-F'''<br /> | '''Golgi alpha-mannosidase II D341N mutant complex with 2-F-mannosyl-F'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The family 38 golgi alpha-mannosidase II, thought to cleave mannosidic | + | 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== | ==About this Structure== | ||
| - | 1QX1 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, FMF 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:// | + | 1QX1 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=FMF:'>FMF</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=1QX1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]] | [[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kuntz, D | + | [[Category: Kuntz, D A.]] |
[[Category: Numao, S.]] | [[Category: Numao, S.]] | ||
| - | [[Category: Rose, D | + | [[Category: Rose, D R.]] |
| - | [[Category: Withers, S | + | [[Category: Withers, S G.]] |
[[Category: FMF]] | [[Category: FMF]] | ||
[[Category: MPD]] | [[Category: MPD]] | ||
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[[Category: glycosyl hydrolase family 38]] | [[Category: glycosyl hydrolase family 38]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:36 2008'' |
Revision as of 12:44, 21 February 2008
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Golgi alpha-mannosidase II D341N mutant complex with 2-F-mannosyl-F
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.
About this Structure
1QX1 is a Single protein structure of sequence from Drosophila melanogaster with , , and as ligands. Active as Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase, with EC number 3.2.1.114 Full crystallographic information is available from OCA.
Reference
Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates., Numao S, Kuntz DA, Withers SG, Rose DR, J Biol Chem. 2003 Nov 28;278(48):48074-83. Epub 2003 Sep 5. PMID:12960159
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