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1fob

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[[Image:1fob.gif|left|200px]]<br /><applet load="1fob" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fob, resolution 1.80&Aring;" />
 
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'''CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 100K'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 100K==
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The three-dimensional structure of Aspergillus aculeatus beta-1,4-galactanase (AAGAL), an enzyme involved in pectin degradation, has been determined by multiple isomorphous replacement to 2.3 and 1.8 A resolution at 293 and 100 K, respectively. It represents the first known structure for a polysaccharidase with this specificity and for a member of glycoside hydrolase family 53 (GH-53). The enzyme folds into a (beta/alpha)(8) barrel with the active site cleft located at the C-terminal side of the barrel consistent with the classification of GH-53 in clan GH-A, a superfamily of enzymes with common fold and catalytic machinery but diverse specificities. Putative substrate-enzyme interactions were elucidated by modeling of beta-1,4-linked galactobioses into the possible substrate binding subsites. The structure and modeling studies identified five potential subsites for the binding of galactans, of which one is a pocket suited for accommodating the arabinan side chain in arabinogalactan, one of the natural substrates. A comparison with the substrate binding grooves of other Clan GH-A enzymes suggests that shape complementarity is crucial in determining the specificity of polysaccharidases.
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<StructureSection load='1fob' size='340' side='right'caption='[[1fob]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fob]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOB 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]] 1.8&#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=CA:CALCIUM+ION'>CA</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=1fob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fob OCA], [https://pdbe.org/1fob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fob RCSB], [https://www.ebi.ac.uk/pdbsum/1fob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fob ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GANA_ASPAC GANA_ASPAC]
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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/fo/1fob_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=1fob 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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1FOB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arabinogalactan_endo-1,4-beta-galactosidase Arabinogalactan endo-1,4-beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.89 3.2.1.89] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOB OCA].
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*[[Beta-1%2C4-galactanase|Beta-1%2C4-galactanase]]
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__TOC__
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==Reference==
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</StructureSection>
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Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A., Ryttersgaard C, Lo Leggio L, Coutinho PM, Henrissat B, Larsen S, Biochemistry. 2002 Dec 24;41(51):15135-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12484750 12484750]
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[[Category: Arabinogalactan endo-1,4-beta-galactosidase]]
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[[Category: Aspergillus aculeatus]]
[[Category: Aspergillus aculeatus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Larsen, S.]]
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[[Category: Larsen S]]
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[[Category: Ryttersgaard, C.]]
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[[Category: Ryttersgaard C]]
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[[Category: CA]]
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[[Category: b/a barrel]]
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[[Category: clan gh-a]]
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[[Category: family 53]]
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[[Category: glycosyl hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:49 2008''
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Current revision

CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 100K

PDB ID 1fob

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