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| - | [[Image:1o4y.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1o4y| PDB=1o4y | SCENE= }} | | {{STRUCTURE_1o4y| PDB=1o4y | SCENE= }} |
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| - | '''THE THREE-DIMENSIONAL STRUCTURE OF BETA-AGARASE A FROM ZOBELLIA GALACTANIVORANS'''
| + | ===THE THREE-DIMENSIONAL STRUCTURE OF BETA-AGARASE A FROM ZOBELLIA GALACTANIVORANS=== |
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| - | ==Overview==
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| - | Agars are important gelifying agents for biochemical use and the food industry. To cleave the beta-1,4-linkages between beta-d-galactose and alpha-l-3,6-anhydro-galactose residues in the red algal galactans known as agars, marine bacteria produce polysaccharide hydrolases called beta-agarases. Beta-agarases A and B from Zobellia galactanivorans Dsij have recently been biochemically characterized. Here we report the first crystal structure of these two beta-agarases. The two proteins were overproduced in Escherichia coli and crystallized, and the crystal structures were determined at 1.48 and 2.3 A for beta-agarases A and B, respectively. The structure of beta-agarase A was solved by the multiple anomalous diffraction method, whereas beta-agarase B was solved with molecular replacement using beta-agarase A as model. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic machinery, namely the nucleophilic residues Glu-147 and Glu-184 and the acid/base residues Glu-152 and Glu-189 for beta-agarases A and B, respectively. The structures of the agarases were compared with those of two lichenases and of a kappa-carrageenase, which all belong to family 16 of the glycoside hydrolases in order to pinpoint the residues responsible for their widely differing substrate specificity. The relationship between structure and enzymatic activity of the two beta-agarases from Z. galactanivorans Dsij was studied by analysis of the degradation products starting with different oligosaccharides. The combination of the structural and biochemical results allowed the determination of the number of subsites present in the catalytic cleft of the beta-agarases.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12970344}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12970344 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12970344}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Cleavage of beta-1]] | | [[Category: Cleavage of beta-1]] |
| | [[Category: Glycoside hydrolase family 16]] | | [[Category: Glycoside hydrolase family 16]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:23:13 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:14:57 2008'' |
Revision as of 00:15, 29 July 2008
Template:STRUCTURE 1o4y
THE THREE-DIMENSIONAL STRUCTURE OF BETA-AGARASE A FROM ZOBELLIA GALACTANIVORANS
Template:ABSTRACT PUBMED 12970344
About this Structure
1O4Y is a Single protein structure of sequence from Zobellia galactanivorans. Full crystallographic information is available from OCA.
Reference
The three-dimensional structures of two beta-agarases., Allouch J, Jam M, Helbert W, Barbeyron T, Kloareg B, Henrissat B, Czjzek M, J Biol Chem. 2003 Nov 21;278(47):47171-80. Epub 2003 Sep 11. PMID:12970344
Page seeded by OCA on Tue Jul 29 03:14:57 2008
