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1uyp
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(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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Revision as of 16:41, 29 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 [[1]], with EC number [3.2.1.26]. 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
Page seeded by OCA on Mon Oct 29 18:45:54 2007
