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| | <StructureSection load='4n2z' size='340' side='right'caption='[[4n2z]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4n2z' size='340' side='right'caption='[[4n2z]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4n2z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Podas Podas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N2Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N2Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4n2z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Podospora_anserina Podospora anserina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N2Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CTR:CELLOTRIOSE'>CTR</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900014:alpha-cellotriose'>PRD_900014</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n1i|4n1i]], [[4n2r|4n2r]], [[4n4b|4n4b]]</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=4n2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n2z OCA], [https://pdbe.org/4n2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n2z RCSB], [https://www.ebi.ac.uk/pdbsum/4n2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n2z ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </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=4n2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n2z OCA], [http://pdbe.org/4n2z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n2z RCSB], [http://www.ebi.ac.uk/pdbsum/4n2z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n2z ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E2GHW5_PODAS E2GHW5_PODAS] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-reducing end alpha-L-arabinofuranosidase]] | + | [[Category: Podospora anserina]] |
| - | [[Category: Podas]]
| + | [[Category: Dumon C]] |
| - | [[Category: Dumon, C]] | + | [[Category: Mourey L]] |
| - | [[Category: Mourey, L]] | + | [[Category: Siguier B]] |
| - | [[Category: Siguier, B]] | + | [[Category: Tranier S]] |
| - | [[Category: Tranier, S]] | + | |
| - | [[Category: Beta-propeller]]
| + | |
| - | [[Category: Hemicellulose binding]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
4n2z is a 1 chain structure with sequence from Podospora anserina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
E2GHW5_PODAS
Publication Abstract from PubMed
alpha-l-Arabinofuranosidases are glycoside hydrolases that specifically hydrolyze non-reducing residues from arabinose-containing polysaccharides. In the case of arabinoxylans, which are the main components of hemicellulose, they are part of microbial xylanolytic systems and are necessary for complete breakdown of arabinoxylans. Glycoside hydrolase family 62 (GH62) is currently a small family of alpha-l-arabinofuranosidases that contains only bacterial and fungal members. Little is known about the GH62 mechanism of action, because only a few members have been biochemically characterized and no three-dimensional structure is available. Here, we present the first crystal structures of two fungal GH62 alpha-l-arabinofuranosidases from the basidiomycete Ustilago maydis (UmAbf62A) and ascomycete Podospora anserina (PaAbf62A). Both enzymes are able to efficiently remove the alpha-l-arabinosyl substituents from arabinoxylan. The overall three-dimensional structure of UmAbf62A and PaAbf62A reveals a five-bladed beta-propeller fold that confirms their predicted classification into clan GH-F together with GH43 alpha-l-arabinofuranosidases. Crystallographic structures of the complexes with arabinose and cellotriose reveal the important role of subsites +1 and +2 for sugar binding. Intriguingly, we observed that PaAbf62A was inhibited by cello-oligosaccharides and displayed binding affinity to cellulose although no activity was observed on a range of cellulosic substrates. Bioinformatic analyses showed that UmAbf62A and PaAbf62A belong to two distinct subfamilies within the GH62 family. The results presented here provide a framework to better investigate the structure-function relationships within the GH62 family.
First Structural Insights into alpha-L-Arabinofuranosidases from the Two GH62 Glycoside Hydrolase Subfamilies.,Siguier B, Haon M, Nahoum V, Marcellin M, Burlet-Schiltz O, Coutinho PM, Henrissat B, Mourey L, O'Donohue MJ, Berrin JG, Tranier S, Dumon C J Biol Chem. 2014 Feb 21;289(8):5261-73. doi: 10.1074/jbc.M113.528133. Epub 2014 , Jan 6. PMID:24394409[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Siguier B, Haon M, Nahoum V, Marcellin M, Burlet-Schiltz O, Coutinho PM, Henrissat B, Mourey L, O'Donohue MJ, Berrin JG, Tranier S, Dumon C. First Structural Insights into alpha-L-Arabinofuranosidases from the Two GH62 Glycoside Hydrolase Subfamilies. J Biol Chem. 2014 Feb 21;289(8):5261-73. doi: 10.1074/jbc.M113.528133. Epub 2014 , Jan 6. PMID:24394409 doi:http://dx.doi.org/10.1074/jbc.M113.528133
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