1uyp

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[[Image:1uyp.gif|left|200px]]
[[Image:1uyp.gif|left|200px]]
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{{Structure
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|PDB= 1uyp |SIZE=350|CAPTION= <scene name='initialview01'>1uyp</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1uyp", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=CAT:Gol+Binding+Site+For+Chain+F'>CAT</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1uyp| PDB=1uyp | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uyp OCA], [http://www.ebi.ac.uk/pdbsum/1uyp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uyp RCSB]</span>
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}}
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'''THE THREE-DIMENSIONAL STRUCTURE OF BETA-FRUCTOSIDASE (INVERTASE) FROM THERMOTOGA MARITIMA'''
'''THE THREE-DIMENSIONAL STRUCTURE OF BETA-FRUCTOSIDASE (INVERTASE) FROM THERMOTOGA MARITIMA'''
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==About this Structure==
==About this Structure==
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1UYP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. This structure supersedes the now removed PDB entry 1UTW. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UYP OCA].
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1UYP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1utw 1utw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UYP OCA].
==Reference==
==Reference==
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[[Category: Henrissat, B.]]
[[Category: Henrissat, B.]]
[[Category: Sulzenbacher, G.]]
[[Category: Sulzenbacher, G.]]
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[[Category: beta-propeller]]
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[[Category: Beta-propeller]]
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[[Category: glycosyl hydrolase family 32]]
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[[Category: Glycosyl hydrolase family 32]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: invertase]]
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[[Category: Invertase]]
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[[Category: sucrose degradation]]
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[[Category: Sucrose degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:52:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:17:13 2008''
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Revision as of 08:52, 3 May 2008

Image:1uyp.gif


PDB ID 1uyp

Drag the structure with the mouse to rotate
1uyp, resolution 1.90Å ()
Ligands: , , ,
Activity: Beta-fructofuranosidase, with EC number 3.2.1.26
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



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 beta-sandwich module. Three carboxylates at the bottom of a deep, negatively charged funnel-shaped depression of the beta-propeller are essential for catalysis and function as nucleophile, general acid, and transition state stabilizer, respectively. The catalytic machinery of invertase is perfectly superimposable to that of the enzymes of families GH43 and GH68. The variation in the position of the furanose ring at the site of cleavage explains the different mechanisms evident in families GH32 and GH68 (retaining) and GH43 (inverting) furanosidases.

About this Structure

1UYP is a Single protein structure of sequence from Thermotoga maritima. This structure supersedes the now removed PDB entry 1utw. 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 Sat May 3 11:52:20 2008

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