1o7a
From Proteopedia
(New page: 200px<br /> <applet load="1o7a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o7a, resolution 2.25Å" /> '''HUMAN BETA-HEXOSAMI...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1O7A is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with NAG, GDL and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O7A OCA]]. | + | 1O7A is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with NAG, GDL and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: ABC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O7A OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12706724 12706724] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12706724 12706724] | ||
| + | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sphingolipid degradation]] | [[Category: sphingolipid degradation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:05:36 2007'' |
Revision as of 12:00, 30 October 2007
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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
Page seeded by OCA on Tue Oct 30 14:05:36 2007
Categories: Beta-N-acetylhexosaminidase | Homo sapiens | Single protein | Klingenstein, R. | Maier, T. | Saenger, W. | Sandhoff, K. | Schuette, C. | Strater, N. | EDO | GDL | NAG | Ba8-barrel | Glycosidase | Glycosyl hydrolase | Hexosaminidase | Lysosomal | Sandhoff disease | Sphingolipid degradation
