4ok4
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.7Å</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='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='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> | ||
</table> | </table> | ||
== Function == | == 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> | [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;"> | ||
| - | == 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. | ||
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| - | 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<ref>PMID:24478312</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4ok4" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal Structure of Alg17c Mutant H202L
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