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| | <StructureSection load='1y9m' size='340' side='right'caption='[[1y9m]], [[Resolution|resolution]] 1.89Å' scene=''> | | <StructureSection load='1y9m' size='340' side='right'caption='[[1y9m]], [[Resolution|resolution]] 1.89Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1y9m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_awamori Aspergillus awamori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y9M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1y9m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_awamori Aspergillus awamori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y9M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y4w|1y4w]], [[1y9g|1y9g]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructan_beta-fructosidase Fructan beta-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.80 3.2.1.80] </span></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=1y9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9m OCA], [https://pdbe.org/1y9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y9m RCSB], [https://www.ebi.ac.uk/pdbsum/1y9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9m ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9m OCA], [http://pdbe.org/1y9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y9m RCSB], [http://www.ebi.ac.uk/pdbsum/1y9m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/INUE_ASPAW INUE_ASPAW] Exo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. Splits off terminal fructose units successively from the non-reducing end of the inulin molecule, and also hydrolyzes levan, stachyose and raffinose.<ref>PMID:11829749</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y9/1y9m_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y9/1y9m_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Aspergillus awamori]] | | [[Category: Aspergillus awamori]] |
| - | [[Category: Fructan beta-fructosidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Eneyskaya, E V]] | + | [[Category: Eneyskaya EV]] |
| - | [[Category: Golubev, A M]] | + | [[Category: Golubev AM]] |
| - | [[Category: Korneeva, O S]] | + | [[Category: Korneeva OS]] |
| - | [[Category: Kulminskaya, A A]] | + | [[Category: Kulminskaya AA]] |
| - | [[Category: Nagem, R A.P]] | + | [[Category: Nagem RAP]] |
| - | [[Category: Neustroev, K N]] | + | [[Category: Neustroev KN]] |
| - | [[Category: Polikarpov, I]] | + | [[Category: Polikarpov I]] |
| - | [[Category: Rojas, A L]] | + | [[Category: Rojas AL]] |
| - | [[Category: Crystallographic structure]]
| + | |
| - | [[Category: Exo-inulinase]]
| + | |
| - | [[Category: Glycoside hydrolase family 32]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Native structure]]
| + | |
| Structural highlights
Function
INUE_ASPAW Exo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. Splits off terminal fructose units successively from the non-reducing end of the inulin molecule, and also hydrolyzes levan, stachyose and raffinose.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Exo-inulinases hydrolyze terminal, non-reducing 2,1-linked and 2,6-linked beta-d-fructofuranose residues in inulin, levan and sucrose releasing beta-d-fructose. We present the X-ray structure at 1.55A resolution of exo-inulinase from Aspergillus awamori, a member of glycoside hydrolase family 32, solved by single isomorphous replacement with the anomalous scattering method using the heavy-atom sites derived from a quick cryo-soaking technique. The tertiary structure of this enzyme folds into two domains: the N-terminal catalytic domain of an unusual five-bladed beta-propeller fold and the C-terminal domain folded into a beta-sandwich-like structure. Its structural architecture is very similar to that of another member of glycoside hydrolase family 32, invertase (beta-fructosidase) from Thermotoga maritima, determined recently by X-ray crystallography The exo-inulinase is a glycoprotein containing five N-linked oligosaccharides. Two crystal forms obtained under similar crystallization conditions differ by the degree of protein glycosylation. The X-ray structure of the enzyme:fructose complex, at a resolution of 1.87A, reveals two catalytically important residues: Asp41 and Glu241, a nucleophile and a catalytic acid/base, respectively. The distance between the side-chains of these residues is consistent with a double displacement mechanism of reaction. Asp189, which is part of the Arg-Asp-Pro motif, provides hydrogen bonds important for substrate recognition.
Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition.,Nagem RA, Rojas AL, Golubev AM, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Neustroev KN, Polikarpov I J Mol Biol. 2004 Nov 19;344(2):471-80. PMID:15522299[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arand M, Golubev AM, Neto JR, Polikarpov I, Wattiez R, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Shabalin KA, Shishliannikov SM, Chepurnaya OV, Neustroev KN. Purification, characterization, gene cloning and preliminary X-ray data of the exo-inulinase from Aspergillus awamori. Biochem J. 2002 Feb 15;362(Pt 1):131-5. PMID:11829749
- ↑ Nagem RA, Rojas AL, Golubev AM, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Neustroev KN, Polikarpov I. Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition. J Mol Biol. 2004 Nov 19;344(2):471-80. PMID:15522299 doi:http://dx.doi.org/10.1016/j.jmb.2004.09.024
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