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1urx

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[[Image:1urx.gif|left|200px]]
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{{STRUCTURE_1urx| PDB=1urx | SCENE= }}
{{STRUCTURE_1urx| PDB=1urx | SCENE= }}
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'''CRYSTALLOGRAPHIC STRUCTURE OF BETA-AGARASE A IN COMPLEX WITH OLIGOAGAROSE'''
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===CRYSTALLOGRAPHIC STRUCTURE OF BETA-AGARASE A IN COMPLEX WITH OLIGOAGAROSE===
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==Overview==
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Agarose is a gel-forming polysaccharide with an alpha-L(1,4)-3,6-anhydro-galactose, beta-D(1,3)-galactose repeat unit, from the cell walls of marine red algae. beta-agarase A, from the Gram-negative bacterium Zobellia galactanivorans, is secreted to the external medium and degrades agarose with an endo-mechanism. The structure of the inactive mutant beta-agarase A-E147S in complex with agaro-octaose has been solved at 1.7 A resolution. Two oligosaccharide chains are bound to the protein. The first one resides in the active site channel, spanning subsites -4 to -1. A second oligosaccharide binding site, on the opposite side of the protein, was filled with eight sugar units, parallel to the active site. The crystal structure of the beta-agarase A with agaro-octaose provides detailed information on agarose recognition in the catalytic site. The presence of the second, parallel, binding site suggests that the enzyme might be able to unwind the double-helical structure of agarose prior to the catalytic cleavage.
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(as it appears on PubMed at http://www.pubmed.gov), where 15062085 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15062085}}
==About this Structure==
==About this Structure==
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[[Category: Glycoside hydrolase]]
[[Category: Glycoside hydrolase]]
[[Category: Two binding-site]]
[[Category: Two binding-site]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:36:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:44:59 2008''

Revision as of 21:45, 27 July 2008

Image:1urx.png

Template:STRUCTURE 1urx

CRYSTALLOGRAPHIC STRUCTURE OF BETA-AGARASE A IN COMPLEX WITH OLIGOAGAROSE

Template:ABSTRACT PUBMED 15062085

About this Structure

1URX is a Single protein structure of sequence from Zobellia galactanivorans. Full crystallographic information is available from OCA.

Reference

Parallel substrate binding sites in a beta-agarase suggest a novel mode of action on double-helical agarose., Allouch J, Helbert W, Henrissat B, Czjzek M, Structure. 2004 Apr;12(4):623-32. PMID:15062085

Page seeded by OCA on Mon Jul 28 00:44:59 2008

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