1gqi

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[[Image:1gqi.gif|left|200px]]
 
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{{Structure
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==Structure of Pseudomonas cellulosa alpha-D-glucuronidase==
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|PDB= 1gqi |SIZE=350|CAPTION= <scene name='initialview01'>1gqi</scene>, resolution 1.48&Aring;
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<StructureSection load='1gqi' size='340' side='right'caption='[[1gqi]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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<table><tr><td colspan='2'>[[1gqi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GQI FirstGlance]. <br>
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|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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqi OCA], [https://pdbe.org/1gqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gqi RCSB], [https://www.ebi.ac.uk/pdbsum/1gqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gqi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AGUA_CELJU 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.<ref>PMID:11937059</ref> <ref>PMID:12169619</ref> <ref>PMID:12654910</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gq/1gqi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gqi ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''STRUCTURE OF PSEUDOMONAS CELLULOSA ALPHA-D-GLUCURONIDASE'''
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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<ref>PMID:11937059</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1gqi" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Glucuronisidase 3D structures|Glucuronisidase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1GQI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQI OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11937059 11937059]
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[[Category: Alpha-glucuronidase]]
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[[Category: Cellvibrio japonicus]]
[[Category: Cellvibrio japonicus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Davies, G J.]]
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[[Category: Davies GJ]]
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[[Category: Gilbert, H J.]]
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[[Category: Gilbert HJ]]
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[[Category: Nagy, T.]]
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[[Category: Nagy T]]
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[[Category: Nurizzo, D.]]
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[[Category: Nurizzo D]]
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[[Category: CO]]
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[[Category: EDO]]
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[[Category: MG]]
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[[Category: (alpha-beta)8 barrel]]
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[[Category: glucuronidase]]
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[[Category: glycoside hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:26:37 2008''
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Current revision

Structure of Pseudomonas cellulosa alpha-D-glucuronidase

PDB ID 1gqi

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