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1o7a

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[[Category: sphingolipid degradation]]
[[Category: sphingolipid degradation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:05:36 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:45:11 2007''

Revision as of 13:40, 30 October 2007

Image:1o7a.gif

1o7a, resolution 2.25Å

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HUMAN BETA-HEXOSAMINIDASE B

Overview

Human lysosomal beta-hexosaminidases are dimeric enzymes composed of alpha, and beta-chains, encoded by the genes HEXA and HEXB. They occur in three, isoforms, the homodimeric hexosaminidases B (betabeta) and S (alphaalpha), and the heterodimeric hexosaminidase A (alphabeta), where dimerization is, required for catalytic activity. Allelic variations in the HEXA and HEXB, genes cause the fatal inborn errors of metabolism Tay-Sachs disease and, Sandhoff disease, respectively. Here, we present the crystal structure of, a complex of human beta-hexosaminidase B with a transition state analogue, inhibitor at 2.3A resolution (pdb 1o7a). On the basis of this structure, and previous studies on related enzymes, a retaining double-displacement, mechanism for glycosyl hydrolysis by ... [(full description)]

About this Structure

1O7A is a [Single protein] structure of sequence from [Homo sapiens] with NAG, GDL and EDO as [ligands]. Active as [Beta-N-acetylhexosaminidase], with EC number [3.2.1.52]. Structure known Active Site: ABC. Full crystallographic information is available from [OCA].

Reference

The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease., Maier T, Strater N, Schuette CG, Klingenstein R, Sandhoff K, Saenger W, J Mol Biol. 2003 May 2;328(3):669-81. PMID:12706724

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