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1mqr

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(New page: 200px<br /><applet load="1mqr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mqr, resolution 2.00&Aring;" /> '''THE CRYSTAL STRUCTUR...)
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[[Image:1mqr.gif|left|200px]]<br /><applet load="1mqr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mqr, resolution 2.00&Aring;" />
 
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'''THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE (E386Q) FROM BACILLUS STEAROTHERMOPHILUS T-6'''<br />
 
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==Overview==
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==THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE (E386Q) FROM BACILLUS STEAROTHERMOPHILUS T-6==
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Alpha-glucuronidases cleave the alpha-1,2-glycosidic bond between, 4-O-methyl-d-glucuronic acid and short xylooligomers as part of the, hemicellulose degradation system. To date, all of the alpha-glucuronidases, are classified as family 67 glycosidases, which catalyze the hydrolysis, via the investing mechanism. Here we describe several high resolution, crystal structures of the alpha-glucuronidase (AguA) from Geobacillus, stearothermophilus, in complex with its substrate and products. In the, complex of AguA with the intact substrate, the 4-O-methyl-d-glucuronic, acid sugar ring is distorted into a half-chair conformation, which is, closer to the planar conformation required for the oxocarbenium ion-like, transition state structure. In the active site, a water molecule is, coordinated between two carboxylic acids, in an appropriate position to, act as a nucleophile. From the structural data it is likely that two, carboxylic acids, Asp(364) and Glu(392), activate together the, nucleophilic water molecule. The loop carrying the catalytic general acid, Glu(285) cannot be resolved in some of the structures but could be, visualized in its "open" and "closed" (catalytic) conformations in other, structures. The protonated state of Glu(285) is presumably stabilized by, its proximity to the negative charge of the substrate, representing a new, variation of substrate-assisted catalysis mechanism.
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<StructureSection load='1mqr' size='340' side='right'caption='[[1mqr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mqr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQR FirstGlance]. <br>
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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]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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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=1mqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mqr OCA], [https://pdbe.org/1mqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mqr RCSB], [https://www.ebi.ac.uk/pdbsum/1mqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mqr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AGUA_GEOSE AGUA_GEOSE] 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 alpha-1,2-glycosidic bond of the 4-O-methyl-D-glucuronic acid side chain of xylan and releases 4-O-methylglucuronic acid from xylan.<ref>PMID:11358519</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/mq/1mqr_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=1mqr ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1MQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MQR OCA].
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*[[Glucuronisidase 3D structures|Glucuronisidase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implications., Golan G, Shallom D, Teplitsky A, Zaide G, Shulami S, Baasov T, Stojanoff V, Thompson A, Shoham Y, Shoham G, J Biol Chem. 2004 Jan 23;279(4):3014-24. Epub 2003 Oct 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14573597 14573597]
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__TOC__
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[[Category: Alpha-glucuronidase]]
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</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Baasov, T.]]
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[[Category: Baasov T]]
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[[Category: Golan, G.]]
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[[Category: Golan G]]
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[[Category: Shallom, D.]]
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[[Category: Shallom D]]
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[[Category: Shoham, G.]]
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[[Category: Shoham G]]
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[[Category: Shoham, Y.]]
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[[Category: Shoham Y]]
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[[Category: Shulami, S.]]
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[[Category: Shulami S]]
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[[Category: Stojanoff, V.]]
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[[Category: Stojanoff V]]
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[[Category: Teplitsky, A.]]
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[[Category: Teplitsky A]]
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[[Category: Thompson, A.]]
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[[Category: Thompson A]]
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[[Category: Zaide, G.]]
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[[Category: Zaide G]]
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[[Category: GOL]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 21:51:14 2007''
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Current revision

THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE (E386Q) FROM BACILLUS STEAROTHERMOPHILUS T-6

PDB ID 1mqr

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