1uyp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1uyp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1uyp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1uyp| PDB=1uyp | SCENE= }}
{{STRUCTURE_1uyp| PDB=1uyp | SCENE= }}
-
'''THE THREE-DIMENSIONAL STRUCTURE OF BETA-FRUCTOSIDASE (INVERTASE) FROM THERMOTOGA MARITIMA'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14973124}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14973124 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14973124}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Invertase]]
[[Category: Invertase]]
[[Category: Sucrose degradation]]
[[Category: Sucrose degradation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:52:20 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:26:57 2008''

Revision as of 07:27, 29 July 2008

Image:1uyp.png


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

Template:ABSTRACT PUBMED 14973124

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 Tue Jul 29 10:26:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uyp"
Personal tools