1urx
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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 .. | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1URX is a | + | 1URX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zobellia_galactanivorans Zobellia galactanivorans] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Beta-agarase Beta-agarase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.81 3.2.1.81] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1URX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: two binding-sites]] | [[Category: two binding-sites]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:41:51 2007'' |
Revision as of 12:36, 5 November 2007
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CRYSTALLOGRAPHIC STRUCTURE OF BETA-AGARASE A IN COMPLEX WITH OLIGOAGAROSE
Overview
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.
About this Structure
1URX is a Single protein structure of sequence from Zobellia galactanivorans with CA as ligand. Active as Beta-agarase, with EC number 3.2.1.81 Structure known Active Site: AC1. 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
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