1c7t

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[[Image:1c7t.gif|left|200px]]
[[Image:1c7t.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1c7t |SIZE=350|CAPTION= <scene name='initialview01'>1c7t</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1c7t", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CBS:DI(N-ACETYL-D-GLUCOSAMINE)'>CBS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1c7t| PDB=1c7t | SCENE= }}
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|RELATEDENTRY=[[1c7s|1C7S]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c7t OCA], [http://www.ebi.ac.uk/pdbsum/1c7t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c7t RCSB]</span>
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}}
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'''BETA-N-ACETYLHEXOSAMINIDASE MUTANT E540D COMPLEXED WITH DI-N ACETYL-D-GLUCOSAMINE (CHITOBIASE)'''
'''BETA-N-ACETYLHEXOSAMINIDASE MUTANT E540D COMPLEXED WITH DI-N ACETYL-D-GLUCOSAMINE (CHITOBIASE)'''
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[[Category: Tavlas, G.]]
[[Category: Tavlas, G.]]
[[Category: Vorgias, C E.]]
[[Category: Vorgias, C E.]]
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[[Category: a/b(tim)-barrel]]
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[[Category: Beta-n-acetylhexosaminidase]]
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[[Category: beta-n-acetylhexosaminidase]]
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[[Category: Chitinolysin]]
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[[Category: chitinolysin]]
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[[Category: Co-crystal structure]]
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[[Category: co-crystal structure]]
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[[Category: Glycosyl hydrolase]]
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[[Category: glycosyl hydrolase]]
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[[Category: Proton donor]]
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[[Category: proton donor]]
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[[Category: Site directed mutagenesis]]
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[[Category: site directed mutagenesis]]
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[[Category: X-ray diffraction]]
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[[Category: x-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:25:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:16:17 2008''
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Revision as of 09:26, 2 May 2008

Image:1c7t.gif

Template:STRUCTURE 1c7t

BETA-N-ACETYLHEXOSAMINIDASE MUTANT E540D COMPLEXED WITH DI-N ACETYL-D-GLUCOSAMINE (CHITOBIASE)


Overview

The catalytic domain of chitobiase (beta-N-1-4 acetylhexosaminidase) from Serratia marcescens, is an alpha/beta TIM-barrel. This enzyme belongs to family 20 of glycosyl hydrolases in which a conserved amino acid pair, aspartate-glutamate, is present (Asp539-Glu540). It was proposed that catalysis by this enzyme family is carried out by glutamate 540 acting as a proton donor and by the acetamido group of the substrate as a nucleophile. We investigated the role of Asp539 and Glu540 by site-directed mutagenesis, biochemical characterization and by structural analyses of chitobiase -substrate co-crystals. We found that both residues are essential for chitobiase activity. The mutations, however, led to subtle changes in the catalytic site. Our results support the model that Glu540 acts as the proton donor and that Asp539 acts in several different ways. Asp539 restrains the acetamido group of the substrate in a specific orientation by forming a hydrogen bond with N2 of the non-reduced (-1) sugar. In addition, this residue participates in substrate binding. It is also required for the correct positioning of Glu540 and may provide additional negative charge at the active site. Thus, these biochemical and structural studies provide a molecular explanation for the functional importance and conservation of these residues.

About this Structure

1C7T is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.

Reference

Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540., Prag G, Papanikolau Y, Tavlas G, Vorgias CE, Petratos K, Oppenheim AB, J Mol Biol. 2000 Jul 14;300(3):611-7. PMID:10884356 Page seeded by OCA on Fri May 2 12:25:59 2008

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