1qba: Difference between revisions
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|PDB= 1qba |SIZE=350|CAPTION= <scene name='initialview01'>1qba</scene>, resolution 1.85Å | |PDB= 1qba |SIZE=350|CAPTION= <scene name='initialview01'>1qba</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <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] | |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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qba OCA], [http://www.ebi.ac.uk/pdbsum/1qba PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qba RCSB]</span> | |||
}} | }} | ||
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[[Category: Vorgias, C E.]] | [[Category: Vorgias, C E.]] | ||
[[Category: Wilson, K S.]] | [[Category: Wilson, K S.]] | ||
[[Category: ba8-barrel]] | [[Category: ba8-barrel]] | ||
[[Category: chitinolysis]] | [[Category: chitinolysis]] | ||
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[[Category: glycosyl hydrolase]] | [[Category: glycosyl hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:11:19 2008'' | ||
Revision as of 20:11, 30 March 2008
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| 1qba, resolution 1.85Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Activity: | Beta-N-acetylhexosaminidase, with EC number 3.2.1.52 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
BACTERIAL CHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20
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
1QBA 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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