1hp4
From Proteopedia
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'''CRYSTAL STRUCTURE OF STREPTOMYCES PLICATUS BETA-N-ACETYLHEXOSAMINIDASE''' | '''CRYSTAL STRUCTURE OF STREPTOMYCES PLICATUS BETA-N-ACETYLHEXOSAMINIDASE''' | ||
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[[Category: Streptomyces plicatus]] | [[Category: Streptomyces plicatus]] | ||
[[Category: Mark, B L.]] | [[Category: Mark, B L.]] | ||
| - | [[Category: | + | [[Category: Family 20]] |
| - | [[Category: | + | [[Category: Glycosyl hydrolase]] |
| - | [[Category: | + | [[Category: Hexosaminidase]] |
| - | [[Category: | + | [[Category: Streptomyces plicatus]] |
| - | [[Category: | + | [[Category: Tim barrel]] |
| - | [[Category: | + | [[Category: X-ray]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:05:13 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:05, 2 May 2008
CRYSTAL STRUCTURE OF STREPTOMYCES PLICATUS BETA-N-ACETYLHEXOSAMINIDASE
Overview
beta-Hexosaminidase, a family 20 glycosyl hydrolase, catalyzes the removal of beta-1,4-linked N-acetylhexosamine residues from oligosaccharides and their conjugates. Heritable deficiency of this enzyme results in various forms of GalNAc-beta(1,4)-[N-acetylneuraminic acid (2,3)]-Gal-beta(1,4)-Glc-ceramide gangliosidosis, including Tay-Sachs disease. We have determined the x-ray crystal structure of a beta-hexosaminidase from Streptomyces plicatus to 2.2 A resolution (Protein Data Bank code ). beta-Hexosaminidases are believed to use a substrate-assisted catalytic mechanism that generates a cyclic oxazolinium ion intermediate. We have solved and refined a complex between the cyclic intermediate analogue N-acetylglucosamine-thiazoline and beta-hexosaminidase from S. plicatus to 2.1 A resolution (Protein Data Bank code ). Difference Fourier analysis revealed the pyranose ring of N-acetylglucosamine-thiazoline bound in the enzyme active site with a conformation close to that of a (4)C(1) chair. A tryptophan-lined hydrophobic pocket envelopes the thiazoline ring, protecting it from solvolysis at the iminium ion carbon. Within this pocket, Tyr(393) and Asp(313) appear important for positioning the 2-acetamido group of the substrate for nucleophilic attack at the anomeric center and for dispersing the positive charge distributed into the oxazolinium ring upon cyclization. This complex provides decisive structural evidence for substrate-assisted catalysis and the formation of a covalent, cyclic intermediate in family 20 beta-hexosaminidases.
About this Structure
1HP4 is a Single protein structure of sequence from Streptomyces plicatus. Full crystallographic information is available from OCA.
Reference
Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase., Mark BL, Vocadlo DJ, Knapp S, Triggs-Raine BL, Withers SG, James MN, J Biol Chem. 2001 Mar 30;276(13):10330-7. Epub 2000 Dec 21. PMID:11124970 Page seeded by OCA on Fri May 2 19:05:13 2008
