1qbb

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[[Image:1qbb.jpg|left|200px]]
[[Image:1qbb.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1qbb |SIZE=350|CAPTION= <scene name='initialview01'>1qbb</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1qbb", 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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-->
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|DOMAIN=
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{{STRUCTURE_1qbb| PDB=1qbb | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qbb OCA], [http://www.ebi.ac.uk/pdbsum/1qbb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qbb RCSB]</span>
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}}
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'''BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG)'''
'''BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG)'''
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[[Category: Vorgias, C E.]]
[[Category: Vorgias, C E.]]
[[Category: Wilson, K S.]]
[[Category: Wilson, K S.]]
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[[Category: ba8-barrel]]
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[[Category: Ba8-barrel]]
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[[Category: chitinolysis]]
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[[Category: Chitinolysis]]
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[[Category: chitobiase]]
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[[Category: Chitobiase]]
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[[Category: glycosyl hydrolase]]
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[[Category: Glycosyl hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:05:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:11:22 2008''
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Revision as of 03:05, 3 May 2008

Template:STRUCTURE 1qbb

BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG)


Overview

Chitin, the second most abundant polysaccharide on earth, is degraded by chitinases and chitobiases. The structure of Serratia marcescens chitobiase has been refined at 1.9 A resolution. The mature protein is folded into four domains and its active site is situated at the C-terminal end of the central (beta alpha)8-barrel. Based on the structure of the complex with the substrate disaccharide chitobiose, we propose an acid-base reaction mechanism, in which only one protein carboxylate acts as catalytic acid, while the nucleophile is the polar acetamido group of the sugar in a substrate-assisted reaction. The structural data lead to the hypothesis that the reaction proceeds with retention of anomeric configuration. The structure allows us to model the catalytic domain of the homologous hexosaminidases to give a structural rationale to pathogenic mutations that underlie Tay-Sachs and Sandhoff disease.

About this Structure

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

Reference

Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease., Tews I, Perrakis A, Oppenheim A, Dauter Z, Wilson KS, Vorgias CE, Nat Struct Biol. 1996 Jul;3(7):638-48. PMID:8673609 Page seeded by OCA on Sat May 3 06:05:43 2008

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