1h4p
From Proteopedia
(New page: 200px<br /> <applet load="1h4p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4p, resolution 1.75Å" /> '''CRYSTAL STRUCTURE O...) |
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==About this Structure== | ==About this Structure== | ||
| - | 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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.58 3.2.1.58]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4P OCA]]. | + | 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== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14730348 14730348] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14730348 14730348] | ||
| + | [[Category: Glucan 1,3-beta-glucosidase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 Tue Oct 30 12:43:11 2007'' |
Revision as of 10:38, 30 October 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 ... [(full description)]
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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