1h4p

From Proteopedia

Revision as of 14:23, 5 November 2007

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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