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1gqj

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Cellvibrio japonicus]]
[[Category: Cellvibrio japonicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Davies, G.J.]]
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[[Category: Davies, G J.]]
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[[Category: Gilbert, H.J.]]
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[[Category: Gilbert, H J.]]
[[Category: Nagy, T.]]
[[Category: Nagy, T.]]
[[Category: Nurizzo, D.]]
[[Category: Nurizzo, D.]]
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[[Category: xylobiose]]
[[Category: xylobiose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:41:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:53 2008''

Revision as of 10:52, 21 February 2008


1gqj, resolution 1.90Å

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STRUCTURE OF PSEUDOMONAS CELLULOSA ALPHA-D-GLUCURONIDASE COMPLEXED WITH XYLOBIOSE

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

1GQJ is a Single protein structure of sequence from Cellvibrio japonicus with and as ligands. Active as Alpha-glucuronidase, with EC number 3.2.1.139 Known structural/functional Site: . 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

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