1urx: Difference between revisions
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[[Image:1urx.gif|left|200px]] | [[Image:1urx.gif|left|200px]] | ||
'''CRYSTALLOGRAPHIC STRUCTURE OF BETA-AGARASE A IN COMPLEX WITH OLIGOAGAROSE''' | {{Structure | ||
|PDB= 1urx |SIZE=350|CAPTION= <scene name='initialview01'>1urx</scene>, resolution 1.7Å | |||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CRYSTALLOGRAPHIC STRUCTURE OF BETA-AGARASE A IN COMPLEX WITH OLIGOAGAROSE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1URX is a [ | 1URX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zobellia_galactanivorans Zobellia galactanivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URX OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15062085 15062085] | ||
[[Category: Beta-agarase]] | [[Category: Beta-agarase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: family 16]] | [[Category: family 16]] | ||
[[Category: glycoside hydrolase]] | [[Category: glycoside hydrolase]] | ||
[[Category: two binding- | [[Category: two binding-site]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:35:54 2008'' | ||
Revision as of 12:35, 20 March 2008
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| 1urx, resolution 1.7Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | CA | ||||||||||||
| Activity: | Beta-agarase, with EC number 3.2.1.81 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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