1urx
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1urx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1urx, resolution 1.7Å" /> '''CRYSTALLOGRAPHIC STR...)
Next diff →
Revision as of 18:29, 29 October 2007
|
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 ... [(full description)]
About this Structure
1URX is a [Single protein] structure of sequence from [Zobellia galactanivorans] with CA as [ligand]. Active as [[1]], with EC number [3.2.1.81]. 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 Oct 29 20:34:01 2007
