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1gql

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Revision as of 06:59, 16 November 2017

Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid and xylotriose

Structural highlights

1gql is a 2 chain structure with sequence from "cellvibrio_cellulosa"_nagy_et_al._2002 "cellvibrio cellulosa" nagy et al. 2002. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1gqi, 1gqj, 1gqk
Activity:	Alpha-glucuronidase, with EC number 3.2.1.139
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AGUA_CELJU] Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. It catalyzes the cleavage of the alpha-1,2-glycosidic bond at the non-reducing end of 4-O-methyl-D-glucuronic acid (4-O-MeGlcA) side chain of short xylooligosaccharides and releases 4-O-methylglucuronic acid. It can also hydrolyze small soluble oligosaccharides such as dobiouronic acid, aldotriouronic acid, aldotetraouronic acid, and aldopentaouronic acid.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nurizzo D, Nagy T, Gilbert HJ, Davies GJ. The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A. Structure. 2002 Apr;10(4):547-56. PMID:11937059
↑ Nagy T, Emami K, Fontes CM, Ferreira LM, Humphry DR, Gilbert HJ. The membrane-bound alpha-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan. J Bacteriol. 2002 Sep;184(17):4925-9. PMID:12169619
↑ Nagy T, Nurizzo D, Davies GJ, Biely P, Lakey JH, Bolam DN, Gilbert HJ. The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants. J Biol Chem. 2003 May 30;278(22):20286-92. Epub 2003 Mar 24. PMID:12654910 doi:10.1074/jbc.M302205200
↑ Nurizzo D, Nagy T, Gilbert HJ, Davies GJ. The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A. Structure. 2002 Apr;10(4):547-56. PMID:11937059

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gql"

@@ Line 1: / Line 1: @@
-==STRUCTURE OF PSEUDOMONAS CELLULOSA ALPHA-D-GLUCURONIDASE COMPLEXED WITH GLUCURONIC ACID AND XYLOTRIOSE==
+==Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid and xylotriose==
 <StructureSection load='1gql' size='340' side='right' caption='[[1gql]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gqi|1gqi]], [[1gqj|1gqj]], [[1gqk|1gqk]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gql OCA], [http://pdbe.org/1gql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gql RCSB], [http://www.ebi.ac.uk/pdbsum/1gql PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gql OCA], [http://pdbe.org/1gql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gql RCSB], [http://www.ebi.ac.uk/pdbsum/1gql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gql ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1gql" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Glucuronidase|Glucuronidase]]
 == References ==
 <references/>

1gql

From Proteopedia

Revision as of 06:59, 16 November 2017

Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid and xylotriose

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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