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1urx
From Proteopedia
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|PDB= 1urx |SIZE=350|CAPTION= <scene name='initialview01'>1urx</scene>, resolution 1.7Å | |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> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=AAL:3,6-ANHYDRO-L-GALACTOSE'>AAL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1urx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1urx OCA], [http://www.ebi.ac.uk/pdbsum/1urx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1urx RCSB]</span> | ||
}} | }} | ||
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[[Category: Helbert, W.]] | [[Category: Helbert, W.]] | ||
[[Category: Henrissat, B.]] | [[Category: Henrissat, B.]] | ||
| - | [[Category: CA]] | ||
[[Category: agarose]] | [[Category: agarose]] | ||
[[Category: beta-agarase]] | [[Category: beta-agarase]] | ||
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[[Category: two binding-site]] | [[Category: two binding-site]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:20 2008'' |
Revision as of 21:14, 30 March 2008
| |||||||
| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Beta-agarase, with EC number 3.2.1.81 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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