1gqi: Difference between revisions
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New page: left|200px<br /> <applet load="1gqi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gqi, resolution 1.48Å" /> '''STRUCTURE OF PSEUDO... |
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== | ==Structure of Pseudomonas cellulosa alpha-D-glucuronidase== | ||
Alpha-glucuronidases, components of an ensemble of enzymes central to the | <StructureSection load='1gqi' size='340' side='right'caption='[[1gqi]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48Å</td></tr> | |||
<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> | |||
<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> | |||
</table> | |||
== Function == | |||
[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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gq/1gqi_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:11937059</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1gqi" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glucuronisidase 3D structures|Glucuronisidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cellvibrio japonicus]] | [[Category: Cellvibrio japonicus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Davies | [[Category: Davies GJ]] | ||
[[Category: Gilbert | [[Category: Gilbert HJ]] | ||
[[Category: Nagy | [[Category: Nagy T]] | ||
[[Category: Nurizzo | [[Category: Nurizzo D]] | ||
