1H and 15N resonance assignments of oxidized flavodoxin from Anacystis nidulans with 3D NMR.
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Clubb RT, Thanabal V, Osborne C, Wagner G
1H and 15N resonance assignments of oxidized flavodoxin from Anacystis nidulans with 3D NMR.
Biochemistry. 1991 Aug 6;30(31):7718-30.
- PubMed ID
- 1907844 [ View in PubMed]
- Abstract
Proton and nitrogen-15 sequence-specific nuclear magnetic resonance assignments have been determined for recombinant oxidized flavodoxin from Anacystis nidulans (169 residues, Mr 19,048). Assignments were obtained by using 15N-1H heteronuclear three-dimensional (3D) NMR spectroscopy on a uniformly nitrogen-15 enriched sample of the protein, pH 6.6, at 30 degrees C. For 165 residues, the backbone and a large fraction of the side-chain proton resonances have been assigned. Medium- and long-range NOE's have been used to characterize the secondary structure. In solution, flavodoxin consists of a five-stranded parallel beta sheet involving residues 3-9, 31-37, 49-56, 81-89, 114-117, and 141-144. Medium-range NOE's indicate the presence of several helices. Several 15N and 1H resonances of the flavin mononucleotide (FMN) prosthetic group have been assigned. The FMN-binding site has been investigated by using polypeptide-FMN NOE's.