1qw9

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(New page: 200px<br /><applet load="1qw9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qw9, resolution 1.20&Aring;" /> '''Crystal structure of...)
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[[Image:1qw9.jpg|left|200px]]<br /><applet load="1qw9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qw9, resolution 1.20&Aring;" />
 
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'''Crystal structure of a family 51 alpha-L-arabinofuranosidase in complex with 4-nitrophenyl-Ara'''<br />
 
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==Overview==
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==Crystal structure of a family 51 alpha-L-arabinofuranosidase in complex with 4-nitrophenyl-Ara==
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High-resolution crystal structures of alpha-L-arabinofuranosidase from, Geobacillus stearothermophilus T-6, a family 51 glycosidase, are, described. The enzyme is a hexamer, and each monomer is organized into two, domains: a (beta/alpha)8-barrel and a 12-stranded beta sandwich with, jelly-roll topology. The structures of the Michaelis complexes with, natural and synthetic substrates, and of the transient covalent, arabinofuranosyl-enzyme intermediate represent two stable states in the, double displacement mechanism, and allow thorough examination of the, catalytic mechanism. The arabinofuranose sugar is tightly bound and, distorted by an extensive network of hydrogen bonds. The two catalytic, residues are 4.7 A apart, and together with other conserved residues, contribute to the stabilization of the oxocarbenium ion-like transition, state via charge delocalization and specific protein-substrate, interactions. The enzyme is an anti-protonator, and a 1.7 A electrophilic, migration of the anomeric carbon takes place during the hydrolysis.
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<StructureSection load='1qw9' size='340' side='right'caption='[[1qw9]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1qw9]] is a 2 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=1QW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QW9 FirstGlance]. <br>
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1QW9 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 KHP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha-N-arabinofuranosidase Alpha-N-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QW9 OCA].
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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]] 1.2&#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=KHP:2-HYDROXYMETHYL-5-(4-NITRO-PHENOXY)-TETRAHYDRO-FURAN-3,4-DIOL'>KHP</scene></td></tr>
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==Reference==
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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=1qw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qw9 OCA], [https://pdbe.org/1qw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qw9 RCSB], [https://www.ebi.ac.uk/pdbsum/1qw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qw9 ProSAT]</span></td></tr>
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Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase., Hovel K, Shallom D, Niefind K, Belakhov V, Shoham G, Baasov T, Shoham Y, Schomburg D, EMBO J. 2003 Oct 1;22(19):4922-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14517232 14517232]
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</table>
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[[Category: Alpha-N-arabinofuranosidase]]
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== Function ==
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[https://www.uniprot.org/uniprot/IABF_GEOSE IABF_GEOSE] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It acts preferentially on aryl-alpha-L-arabinofuranosides, and is much less effective on aryl-beta-D-xylopyranosides.<ref>PMID:11943144</ref> <ref>PMID:12221104</ref> <ref>PMID:14517232</ref> <ref>PMID:7887599</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/qw/1qw9_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=1qw9 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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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: Bassov, T.]]
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[[Category: Bassov T]]
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[[Category: Belakhov, V.]]
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[[Category: Belakhov V]]
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[[Category: Hoevel, K.]]
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[[Category: Hoevel K]]
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[[Category: Niefind, K.]]
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[[Category: Niefind K]]
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[[Category: Schomburg, D.]]
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[[Category: Schomburg D]]
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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: KHP]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:03:29 2007''
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Current revision

Crystal structure of a family 51 alpha-L-arabinofuranosidase in complex with 4-nitrophenyl-Ara

PDB ID 1qw9

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