1gqi
From Proteopedia
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|PDB= 1gqi |SIZE=350|CAPTION= <scene name='initialview01'>1gqi</scene>, resolution 1.48Å | |PDB= 1gqi |SIZE=350|CAPTION= <scene name='initialview01'>1gqi</scene>, resolution 1.48Å | ||
|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-glucuronidase Alpha-glucuronidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.139 3.2.1.139] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucuronidase Alpha-glucuronidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.139 3.2.1.139] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqi OCA], [http://www.ebi.ac.uk/pdbsum/1gqi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gqi RCSB]</span> | ||
}} | }} | ||
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[[Category: Nagy, T.]] | [[Category: Nagy, T.]] | ||
[[Category: Nurizzo, D.]] | [[Category: Nurizzo, D.]] | ||
| - | [[Category: CO]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: MG]] | ||
[[Category: (alpha-beta)8 barrel]] | [[Category: (alpha-beta)8 barrel]] | ||
[[Category: glucuronidase]] | [[Category: glucuronidase]] | ||
[[Category: glycoside hydrolase]] | [[Category: glycoside hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:49:19 2008'' |
Revision as of 17:49, 30 March 2008
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| , resolution 1.48Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Alpha-glucuronidase, with EC number 3.2.1.139 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF PSEUDOMONAS CELLULOSA ALPHA-D-GLUCURONIDASE
Overview
Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. The structure of the alpha-glucuronidase, GlcA67A, from Pseudomonas cellulosa reveals three domains, the central of which is a (beta/alpha)(8) barrel housing the catalytic apparatus. Complexes of the enzyme with the individual reaction products, either xylobiose or glucuronic acid, and the ternary complex of both glucuronic acid and xylotriose reveal a "blind" pocket which selects for short decorated xylooligosaccharides substituted with the uronic acid at their nonreducing end, consistent with kinetic data. The catalytic center reveals a constellation of carboxylates; Glu292 is poised to provide protonic assistance to leaving group departure with Glu393 and Asp365 both appropriately positioned to provide base-catalyzed assistance for inverting nucleophilic attack by water.
About this Structure
1GQI is a Single protein structure of sequence from Cellvibrio japonicus. Full crystallographic information is available from OCA.
Reference
The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A., Nurizzo D, Nagy T, Gilbert HJ, Davies GJ, Structure. 2002 Apr;10(4):547-56. PMID:11937059
Page seeded by OCA on Sun Mar 30 20:49:19 2008
