1qbb

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1qbb, resolution 2.00Å

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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 with CBS and SO4 as ligands. Active as Beta-N-acetylhexosaminidase, with EC number 3.2.1.52 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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