1urx
From Proteopedia
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| - | [[Image:1urx.gif|left|200px]]<br /> | + | [[Image:1urx.gif|left|200px]]<br /><applet load="1urx" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1urx" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1urx, resolution 1.7Å" /> | caption="1urx, resolution 1.7Å" /> | ||
'''CRYSTALLOGRAPHIC STRUCTURE OF BETA-AGARASE A IN COMPLEX WITH OLIGOAGAROSE'''<br /> | '''CRYSTALLOGRAPHIC STRUCTURE OF BETA-AGARASE A IN COMPLEX WITH OLIGOAGAROSE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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] | + | 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] Known structural/functional Site: <scene name='pdbsite=AC1:Ca Binding Site For Chain A'>AC1</scene>. 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 Tue Dec 18 18:08:35 2007'' |
Revision as of 15:58, 18 December 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 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 Known structural/functional Site: . 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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