2ml3

Solution Structure of AlgE6R3 subunit from the Azotobacter vinelandii Mannuronan C5-epimerase

spinqualitylabelsall models 2ml3 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ml3 is a 1 chain structure with sequence from Azotobacter vinelandii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. Publication Abstract from PubMed 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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