2ml3
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ml3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ML3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ML3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ml3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ML3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ML3 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pyg|2pyg]], [[2pyh|2pyh]], [[2agm|2agm]], [[2ml1|2ml1]], [[2ml2|2ml2]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pyg|2pyg]], [[2pyh|2pyh]], [[2agm|2agm]], [[2ml1|2ml1]], [[2ml2|2ml2]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ml3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ml3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ml3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ml3 PDBsum]</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=2ml3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ml3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ml3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ml3 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ALGE6_AZOVI ALGE6_AZOVI]] Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), producing a polymer with gel-forming capacity, required for the formation of the cyst coat. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | The | + | The bacterium Azotobacter vinelandii produces a family of seven secreted and calcium-dependent mannuronan C-5 epimerases (AlgE1-7). These epimerases are responsible for the epimerization of beta-d-mannuronic acid (M) to alpha-l-guluronic acid (G) in alginate polymers. The epimerases display a modular structure composed of one or two catalytic A-modules and from one to seven R-modules having an activating effect on the A-module. In this study, we have determined the NMR structure of the three individual R-modules from AlgE6 (AR1R2R3) and the overall structure of both AlgE4 (AR) and AlgE6 using small angle x-ray scattering. Furthermore, the alginate binding ability of the R-modules of AlgE4 and AlgE6 has been studied with NMR and isothermal titration calorimetry. The AlgE6 R-modules fold into an elongated parallel beta-roll with a shallow, positively charged groove across the module. Small angle x-ray scattering analyses of AlgE4 and AlgE6 show an overall elongated shape with some degree of flexibility between the modules for both enzymes. Titration of the R-modules with defined alginate oligomers shows strong interaction between AlgE4R and both oligo-M and MG, whereas no interaction was detected between these oligomers and the individual R-modules from AlgE6. A combination of all three R-modules from AlgE6 shows weak interaction with long M-oligomers. Exchanging the R-modules between AlgE4 and AlgE6 resulted in a novel epimerase called AlgE64 with increased G-block forming ability compared with AlgE6. |
| - | + | Structural and Functional Characterization of the R-modules in Alginate C-5 Epimerases AlgE4 and AlgE6 from Azotobacter vinelandii.,Buchinger E, Knudsen DH, Behrens MA, Pedersen JS, Aarstad OA, Tondervik A, Valla S, Skjak-Braek G, Wimmer R, Aachmann FL J Biol Chem. 2014 Nov 7;289(45):31382-96. doi: 10.1074/jbc.M114.567008. Epub 2014, Sep 29. PMID:25266718<ref>PMID:25266718</ref> | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Aachmann, F L | + | [[Category: Aachmann, F L]] |
| - | [[Category: Buchinger, E | + | [[Category: Buchinger, E]] |
| - | [[Category: Wimmer, R | + | [[Category: Wimmer, R]] |
[[Category: Alginate c-5 epimerase]] | [[Category: Alginate c-5 epimerase]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Mannuronan c-5 epimerase]] | [[Category: Mannuronan c-5 epimerase]] | ||
[[Category: R-module]] | [[Category: R-module]] | ||
Revision as of 10:52, 24 December 2014
Solution Structure of AlgE6R3 subunit from the Azotobacter vinelandii Mannuronan C5-epimerase
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