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| | <StructureSection load='3ziz' size='340' side='right'caption='[[3ziz]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='3ziz' size='340' side='right'caption='[[3ziz]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ziz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Podas Podas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZIZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ziz]] 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=3ZIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZIZ FirstGlance]. <br> |
| - | </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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zm8|3zm8]]</div></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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </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=3ziz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ziz OCA], [https://pdbe.org/3ziz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ziz RCSB], [https://www.ebi.ac.uk/pdbsum/3ziz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ziz ProSAT]</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=3ziz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ziz OCA], [https://pdbe.org/3ziz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ziz RCSB], [https://www.ebi.ac.uk/pdbsum/3ziz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ziz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MANA_PODAN MANA_PODAN] Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Hydrolyzes structurally different mannan polysaccharides, such as galactomannans, glucomannans, and beta-1,4-mannans from different sources, yielding principally mannobiose (PubMed:21037302). Also has transglycosylation activity (PubMed:23558681).<ref>PMID:21037302</ref> <ref>PMID:23558681</ref> |
| | <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: Mannan endo-1,4-beta-mannosidase]] | + | [[Category: Podospora anserina]] |
| - | [[Category: Podas]]
| + | [[Category: Berrin JG]] |
| - | [[Category: Berrin, J G]] | + | [[Category: Couturier M]] |
| - | [[Category: Couturier, M]] | + | [[Category: Leone P]] |
| - | [[Category: Leone, P]] | + | [[Category: Rosengren A]] |
| - | [[Category: Rosengren, A]] | + | [[Category: Roussel A]] |
| - | [[Category: Roussel, A]] | + | [[Category: Stalbrand H]] |
| - | [[Category: Stalbrand, H]] | + | |
| - | [[Category: Cazy]]
| + | |
| - | [[Category: Glycosyl hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mannanase]]
| + | |
| Structural highlights
Function
MANA_PODAN Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Hydrolyzes structurally different mannan polysaccharides, such as galactomannans, glucomannans, and beta-1,4-mannans from different sources, yielding principally mannobiose (PubMed:21037302). Also has transglycosylation activity (PubMed:23558681).[1] [2]
Publication Abstract from PubMed
The microbial deconstruction of the plant cell wall is a key biological process that is of increasing importance with the development of a sustainable biofuel industry. The glycoside hydrolase families GH5 (PaMan5A) and GH26 (PaMan26A) endo-beta-1,4-mannanases from the coprophilic ascomycete Podospora anserina contribute to the enzymatic degradation of lignocellulosic biomass. In this study, P. anserina mannanases were further subjected to detailed comparative analysis of their substrate specificities, active site organization and transglycosylation capacity. Although PaMan5A displays a classical mode of action, PaMan26A revealed an atypical hydrolysis pattern with the release of mannotetraose and mannose from mannopentaose resulting from a predominant binding mode involving the -4 subsite. The crystal structures of PaMan5A and PaMan26A were solved at 1.4A and 2.85A resolution, respectively. Analysis of the PaMan26A structure supported strong interaction with substrate at the -4 subsite mediated by two aromatic residues W244 and W245. The PaMan26A structure appended to its family 35 carbohydrate-binding module revealed a short and proline-rich rigid linker that anchored together the catalytic and the binding modules.
Structural and biochemical analyses of glycoside hydrolase families 5 and 26 beta-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharides catalysis.,Couturier M, Roussel A, Rosengren A, Leone P, Stalbrand H, Berrin JG J Biol Chem. 2013 Apr 4. PMID:23558681[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Couturier M, Haon M, Coutinho PM, Henrissat B, Lesage-Meessen L, Berrin JG. Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass. Appl Environ Microbiol. 2011 Jan;77(1):237-46. PMID:21037302 doi:10.1128/AEM.01761-10
- ↑ Couturier M, Roussel A, Rosengren A, Leone P, Stalbrand H, Berrin JG. Structural and biochemical analyses of glycoside hydrolase families 5 and 26 beta-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharides catalysis. J Biol Chem. 2013 Apr 4. PMID:23558681 doi:10.1074/jbc.M113.459438
- ↑ Couturier M, Roussel A, Rosengren A, Leone P, Stalbrand H, Berrin JG. Structural and biochemical analyses of glycoside hydrolase families 5 and 26 beta-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharides catalysis. J Biol Chem. 2013 Apr 4. PMID:23558681 doi:10.1074/jbc.M113.459438
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