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| | ==Crystal Structure of Alg17c Mutant H202L== | | ==Crystal Structure of Alg17c Mutant H202L== |
| - | <StructureSection load='4ok4' size='340' side='right' caption='[[4ok4]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='4ok4' size='340' side='right'caption='[[4ok4]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ok4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Microbulbifer_degradans_2-40 Microbulbifer degradans 2-40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OK4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OK4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ok4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharophagus_degradans_2-40 Saccharophagus degradans 2-40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OK4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ojz|4ojz]], [[4ok2|4ok2]]</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=4ok4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ok4 OCA], [https://pdbe.org/4ok4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ok4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ok4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ok4 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alg17A, alg17C, Sde_3284 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=203122 Microbulbifer degradans 2-40])</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=4ok4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ok4 OCA], [http://pdbe.org/4ok4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ok4 RCSB], [http://www.ebi.ac.uk/pdbsum/4ok4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ok4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/EALGL_SACD2 EALGL_SACD2] Catalyzes the depolymerization of alginate through an exolytic mode of action, via a beta-elimination mechanism. Preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid.<ref>PMID:22281843</ref> <ref>PMID:24478312</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Microbulbifer degradans 2-40]] | + | [[Category: Large Structures]] |
| - | [[Category: Nair, S K]] | + | [[Category: Saccharophagus degradans 2-40]] |
| - | [[Category: Park, D S]] | + | [[Category: Nair SK]] |
| - | [[Category: Alginate lyase]] | + | [[Category: Park DS]] |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
EALGL_SACD2 Catalyzes the depolymerization of alginate through an exolytic mode of action, via a beta-elimination mechanism. Preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid.[1] [2]
Publication Abstract from PubMed
Brown macroalgae represent an ideal source for complex polysaccharides that can be utilized as precursors for cellulosic biofuels. The lack of recalcitrant lignin components in macroalgae polysaccharide reserves provides a facile route for depolymerization of constituent polysaccharides into simple monosaccharides. The most abundant sugars in macroalgae are alginate, mannitol, and glucan, and although several classes of enzymes that can catabolize the latter two have been characterized, studies of alginate-depolymerizing enzymes have lagged. Here, we present several crystal structures of Alg17c from marine bacterium Saccharophagus degradans along with structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization. This represents the first structural and biochemical characterization of a family 17 polysaccharide lyase enzyme. Despite the lack of appreciable sequence conservation, the structure and beta-elimination mechanism for glycolytic bond cleavage by Alg17c are similar to those observed for family 15 polysaccharide lyases and other lyases. This work illuminates the evolutionary relationships among enzymes within this unexplored class of polysaccharide lyases and reinforces the notion of a structure-based hierarchy in the classification of these enzymes.
Structure of a PL17 Family Alginate Lyase Demonstrates Functional Similarities among Exotype Depolymerases.,Park D, Jagtap S, Nair SK J Biol Chem. 2014 Mar 21;289(12):8645-55. doi: 10.1074/jbc.M113.531111. Epub 2014, Jan 29. PMID:24478312[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim HT, Chung JH, Wang D, Lee J, Woo HC, Choi IG, Kim KH. Depolymerization of alginate into a monomeric sugar acid using Alg17C, an exo-oligoalginate lyase cloned from Saccharophagus degradans 2-40. Appl Microbiol Biotechnol. 2012 Mar;93(5):2233-9. doi: 10.1007/s00253-012-3882-x. , Epub 2012 Jan 27. PMID:22281843 doi:http://dx.doi.org/10.1007/s00253-012-3882-x
- ↑ Park D, Jagtap S, Nair SK. Structure of a PL17 Family Alginate Lyase Demonstrates Functional Similarities among Exotype Depolymerases. J Biol Chem. 2014 Mar 21;289(12):8645-55. doi: 10.1074/jbc.M113.531111. Epub 2014, Jan 29. PMID:24478312 doi:http://dx.doi.org/10.1074/jbc.M113.531111
- ↑ Park D, Jagtap S, Nair SK. Structure of a PL17 Family Alginate Lyase Demonstrates Functional Similarities among Exotype Depolymerases. J Biol Chem. 2014 Mar 21;289(12):8645-55. doi: 10.1074/jbc.M113.531111. Epub 2014, Jan 29. PMID:24478312 doi:http://dx.doi.org/10.1074/jbc.M113.531111
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