1qbb
From Proteopedia
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| - | [[Image:1qbb.jpg|left|200px]] | + | [[Image:1qbb.jpg|left|200px]] |
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| - | '''BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG)''' | + | {{Structure |
| + | |PDB= 1qbb |SIZE=350|CAPTION= <scene name='initialview01'>1qbb</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CBS:DI(N-ACETYL-D-GLUCOSAMINE)'>CBS</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QBB is a [ | + | 1QBB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QBB OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8673609 8673609] |
[[Category: Beta-N-acetylhexosaminidase]] | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
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[[Category: glycosyl hydrolase]] | [[Category: glycosyl hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:35:23 2008'' |
Revision as of 11:35, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Beta-N-acetylhexosaminidase, with EC number 3.2.1.52 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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