1uyp
From Proteopedia
(New page: 200px<br /> <applet load="1uyp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uyp, resolution 1.90Å" /> '''THE THREE-DIMENSION...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1UYP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]] with SO4, NA, CIT and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. This structure superseeds the now removed PDB entry 1UTW. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.26 3.2.1.26]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UYP OCA]]. | + | 1UYP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]] with SO4, NA, CIT and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. This structure superseeds the now removed PDB entry 1UTW. Active as [[http://en.wikipedia.org/wiki/Beta-fructofuranosidase Beta-fructofuranosidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.26 3.2.1.26]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UYP OCA]]. |
==Reference== | ==Reference== | ||
The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases., Alberto F, Bignon C, Sulzenbacher G, Henrissat B, Czjzek M, J Biol Chem. 2004 Apr 30;279(18):18903-10. Epub 2004 Feb 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14973124 14973124] | The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases., Alberto F, Bignon C, Sulzenbacher G, Henrissat B, Czjzek M, J Biol Chem. 2004 Apr 30;279(18):18903-10. Epub 2004 Feb 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14973124 14973124] | ||
| + | [[Category: Beta-fructofuranosidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: sucrose degradation]] | [[Category: sucrose 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 12:04:16 2007'' |
Revision as of 09:59, 30 October 2007
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THE THREE-DIMENSIONAL STRUCTURE OF BETA-FRUCTOSIDASE (INVERTASE) FROM THERMOTOGA MARITIMA
Overview
Thermotoga maritima invertase (beta-fructosidase) hydrolyzes sucrose to, release fructose and glucose, which are major carbon and energy sources, for both prokaryotes and eukaryotes. The name "invertase" was given to, this enzyme over a century ago, because the 1:1 mixture of glucose and, fructose that it produces was named "invert sugar." Despite its name, the, enzyme operates with a mechanism leading to the retention of the anomeric, configuration at the site of cleavage. The enzyme belongs to family GH32, of the sequence-based classification of glycosidases. The crystal, structure, determined at 2-A resolution, reveals two modules, namely a, five-bladed beta-propeller with structural similarity to the, beta-propeller structures of glycosidase from families GH43 and GH68, connected to a ... [(full description)]
About this Structure
1UYP is a [Single protein] structure of sequence from [Thermotoga maritima] with SO4, NA, CIT and GOL as [ligands]. This structure superseeds the now removed PDB entry 1UTW. Active as [Beta-fructofuranosidase], with EC number [3.2.1.26]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases., Alberto F, Bignon C, Sulzenbacher G, Henrissat B, Czjzek M, J Biol Chem. 2004 Apr 30;279(18):18903-10. Epub 2004 Feb 18. PMID:14973124
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