1urx: Difference between revisions
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'''CRYSTALLOGRAPHIC STRUCTURE OF BETA-AGARASE A IN COMPLEX WITH OLIGOAGAROSE''' | '''CRYSTALLOGRAPHIC STRUCTURE OF BETA-AGARASE A IN COMPLEX WITH OLIGOAGAROSE''' | ||
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[[Category: Helbert, W.]] | [[Category: Helbert, W.]] | ||
[[Category: Henrissat, B.]] | [[Category: Henrissat, B.]] | ||
[[Category: | [[Category: Agarose]] | ||
[[Category: | [[Category: Beta-agarase]] | ||
[[Category: | [[Category: Double helix]] | ||
[[Category: | [[Category: Family 16]] | ||
[[Category: | [[Category: Glycoside hydrolase]] | ||
[[Category: | [[Category: Two binding-site]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:36:22 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 08:36, 3 May 2008
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. 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 Sat May 3 11:36:22 2008
