1hcu
From Proteopedia
(New page: 200px<br /> <applet load="1hcu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hcu, resolution 2.37Å" /> '''ALPHA-1,2-MANNOSIDA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1HCU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ | + | 1HCU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]] with NAG and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,2-alpha-mannosidase Mannosyl-oligosaccharide 1,2-alpha-mannosidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.113 3.2.1.113]]. Structure known Active Site: CAA. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HCU OCA]]. |
==Reference== | ==Reference== | ||
Trichoderma reesei alpha-1,2-mannosidase: structural basis for the cleavage of four consecutive mannose residues., Van Petegem F, Contreras H, Contreras R, Van Beeumen J, J Mol Biol. 2001 Sep 7;312(1):157-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11545593 11545593] | Trichoderma reesei alpha-1,2-mannosidase: structural basis for the cleavage of four consecutive mannose residues., Van Petegem F, Contreras H, Contreras R, Van Beeumen J, J Mol Biol. 2001 Sep 7;312(1):157-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11545593 11545593] | ||
| + | [[Category: Hypocrea jecorina]] | ||
| + | [[Category: Mannosyl-oligosaccharide 1,2-alpha-mannosidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Trichoderma reesei]] | ||
[[Category: Beeumen, J.Van.]] | [[Category: Beeumen, J.Van.]] | ||
[[Category: Contreras, H.]] | [[Category: Contreras, H.]] | ||
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[[Category: glycosylation]] | [[Category: glycosylation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:27:34 2007'' |
Revision as of 10:22, 30 October 2007
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ALPHA-1,2-MANNOSIDASE FROM TRICHODERMA REESEI
Overview
The process of N-glycosylation of eukaryotic proteins involves a range of, host enzymes that delete or add saccharide monomers. While endoplasmic, reticulum (E.R.) mannosidases cleave only one mannose to produce the Man8B, isomer, an alpha-1,2-mannosidase from Trichoderma reesei can sequentially, cleave all four 1,2-linked mannose sugars from a Man(9)GlcNAc(2), oligosaccharide, a feature reminiscent of the activity of Golgi, mannosidases. We now report the structure of the T. reesei enzyme at 2.37, A resolution. The enzyme folds as an (alpha alpha)(7) barrel. The, substrate-binding site of the T. reesei mannosidase differs appreciably, from the Saccharomyces cerevisiae enzyme. In the former, shorter loops at, the surface allow substrate protein to come closer to the catalytic site., There ... [(full description)]
About this Structure
1HCU is a [Single protein] structure of sequence from [Hypocrea jecorina] with NAG and CA as [ligands]. Active as [Mannosyl-oligosaccharide 1,2-alpha-mannosidase], with EC number [3.2.1.113]. Structure known Active Site: CAA. Full crystallographic information is available from [OCA].
Reference
Trichoderma reesei alpha-1,2-mannosidase: structural basis for the cleavage of four consecutive mannose residues., Van Petegem F, Contreras H, Contreras R, Van Beeumen J, J Mol Biol. 2001 Sep 7;312(1):157-65. PMID:11545593
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