NMR assignments of 1H, 13C and 15N resonances of the C-terminal subunit from Azotobacter vinelandii mannuronan C5-epimerase 6 (AlgE6R3)
نویسندگان
چکیده
The 19.9 kDa C-terminal module (R3) from Azotobacter vinelandii mannronan C5-epimerase AlgE6 has been (13)C, (15)N isotopically labelled and recombinantly expressed. We report here the (1)H, (13)C, (15)N resonance assignment of AlgE6R3.
منابع مشابه
1H, 13C and 15N resonances of the AlgE62 subunit from Azotobacter vinelandii mannuronan C5-epimerase
The 17.7 kDa R2 module from Azotobacter vinelandii mannronan C5-epimerase AlgE6 has been isotopically labeled ((13)C,(15)N) and recombinantly expressed. Here we report the (1)H, (13)C, (15)N resonance assignment of AlgE6R2.
متن کاملStructure elucidation of azotobactin 87, isolated from Azotobacter vinelandii ATCC 12837.
Chromopeptide siderophores (azotobactin 87-I and -II) were isolated from an iron deficient culture medium of Azotobacter vinelandii ATCC 12837 (= DSM 87). Their structures were elucidated by chemical degradation studies and spectroscopic methods, especially 2D-NMR-techniques. Total assignments of 1H-, 13C-, and 15N-resonances based on 2D-HOHAHA-, 1H/13C-HMQC-, 1H/13C-HMBC-, 1H/15N-HMQC/TOCSY-, ...
متن کاملBiochemical analysis of the processive mechanism for epimerization of alginate by mannuronan C-5 epimerase AlgE4.
The enzymes mannuronan C-5 epimerases catalyse the in-chain epimerisation of beta-D-mannuronic acid to alpha-L-guluronic acid in the last step of alginate biosynthesis. The recombinant C-5 epimerase AlgE4, encoded by the soil bacteria Azotobacter vinelandii and expressed in Escherichia coli, exhibits a non-random mode of action when acting on mannuronan and alginates of various monomeric compos...
متن کاملPossible role of a short extra loop of the long-chain flavodoxin from Azotobacter chroococcum in electron transfer to nitrogenase: complete 1H, 15N and 13C backbone assignments and secondary solution structure of the flavodoxin.
The 1H, 15N and 13C backbone and 1H and 13C beta resonance assignments of the long-chain flavodoxin from Azotobacter chroococcum (the 20-kDa nifF product, flavodoxin-2) in its oxidized form were made at pH 6.5 and 30 degrees C using heteronuclear multidimensional NMR spectroscopy. Analysis of the NOE connectivities, together with amide exchange rates, 3JHNH alpha coupling constants and secondar...
متن کاملBackbone assignments and secondary structure of the Escherichia coli enzyme-II mannitol A domain determined by heteronuclear three-dimensional NMR spectroscopy.
This report presents the backbone assignments and the secondary structure determination of the A domain of the Escherichia coli mannitol transport protein, enzyme-IImtl. The backbone resonances were partially assigned using three-dimensional heteronuclear 1H NOE 1H-15N single-quantum coherence (15N NOESY-HSQC) spectroscopy and three-dimensional heteronuclear 1H total correlation 1H-15N single-q...
متن کامل