1h4p
From Proteopedia
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==Overview== | ==Overview== | ||
| - | We present in vitro data that explain the recognition mechanism of, misfolded glycoproteins by UDP-glucose glycoprotein-glucosyltransferase, (UGGT). The glycoprotein exo-(1,3)-beta-glucanase (beta-Glc) bearing two, glycans unfolds in a pH-dependent manner to become a misfolded substrate, for UGGT. In the crystal structure of this glycoprotein, the local, hydrophobicity surrounding each glycosylation site coincides with the, differential recognition of N-linked glycans by UGGT. We introduced a, single F280S point mutation, producing a beta-Glc protein with full, enzymatic activity that was both recognized as misfolded and, monoglucosylated by UGGT. Contrary to current views, these data show that, UGGT can modify N-linked glycans positioned at least 40 A from localized, regions of disorder . | + | We present in vitro data that explain the recognition mechanism of, misfolded glycoproteins by UDP-glucose glycoprotein-glucosyltransferase, (UGGT). The glycoprotein exo-(1,3)-beta-glucanase (beta-Glc) bearing two, glycans unfolds in a pH-dependent manner to become a misfolded substrate, for UGGT. In the crystal structure of this glycoprotein, the local, hydrophobicity surrounding each glycosylation site coincides with the, differential recognition of N-linked glycans by UGGT. We introduced a, single F280S point mutation, producing a beta-Glc protein with full, enzymatic activity that was both recognized as misfolded and, monoglucosylated by UGGT. Contrary to current views, these data show that, UGGT can modify N-linked glycans positioned at least 40 A from localized, regions of disorder and sense subtle conformational changes within, structurally compact, enzymatically active glycoprotein substrates. |
==About this Structure== | ==About this Structure== | ||
| - | 1H4P is a | + | 1H4P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucan_1,3-beta-glucosidase Glucan 1,3-beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.58 3.2.1.58] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolyase]] | [[Category: hydrolyase]] | ||
| - | ''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 14:10:52 2007'' |
Revision as of 12:05, 5 November 2007
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CRYSTAL STRUCTURE OF EXO-1,3-BETA GLUCANSE FROM SACCHAROMYCES CEREVISIAE
Overview
We present in vitro data that explain the recognition mechanism of, misfolded glycoproteins by UDP-glucose glycoprotein-glucosyltransferase, (UGGT). The glycoprotein exo-(1,3)-beta-glucanase (beta-Glc) bearing two, glycans unfolds in a pH-dependent manner to become a misfolded substrate, for UGGT. In the crystal structure of this glycoprotein, the local, hydrophobicity surrounding each glycosylation site coincides with the, differential recognition of N-linked glycans by UGGT. We introduced a, single F280S point mutation, producing a beta-Glc protein with full, enzymatic activity that was both recognized as misfolded and, monoglucosylated by UGGT. Contrary to current views, these data show that, UGGT can modify N-linked glycans positioned at least 40 A from localized, regions of disorder and sense subtle conformational changes within, structurally compact, enzymatically active glycoprotein substrates.
About this Structure
1H4P is a Single protein structure of sequence from Saccharomyces cerevisiae with GOL as ligand. Active as Glucan 1,3-beta-glucosidase, with EC number 3.2.1.58 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation., Taylor SC, Ferguson AD, Bergeron JJ, Thomas DY, Nat Struct Mol Biol. 2004 Feb;11(2):128-34. Epub 2004 Jan 4. PMID:14730348
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