1hcu: Difference between revisions
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==Overview== | ==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 .. | 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 is more internal space available, so that different oligosaccharide, conformations are sterically allowed in the T. reesei, alpha-1,2-mannosidase. | ||
==About this Structure== | ==About this Structure== | ||
1HCU is a | 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== | ||
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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 Mon Nov 5 13:59:35 2007'' | ||
