1H and 15N resonance assignments of oxidized flavodoxin from Anacystis nidulans with 3D NMR.
Related Articles 1H and 15N resonance assignments of oxidized flavodoxin from Anacystis nidulans with 3D NMR.
Biochemistry. 1991 Aug 6;30(31):7718-30
Authors: Clubb RT, Thanabal V, Osborne C, Wagner G
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.
PMID: 1907844 [PubMed - indexed for MEDLINE]
Source:
PubMed