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sup 1 H and sup 15 N resonance assignments of oxidized flavodoxin from Anacystis nidulans with 3D NMR

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00245a008· OSTI ID:5602898
 [1]; ;  [2];  [3]
  1. Univ. of Michigan, Ann Arbor (United States) Harvard Medical School, Boston, MA (United States)
  2. Univ. of Michigan, Ann Arbor (United States)
  3. Harvard Medical School, Boston, MA (United States)

Proton and nitrogen-15 sequence-specific nuclear magnetic resonance assignments have been determined for recombinant oxidized flavodoxin from Anacystis nidulans. Assignments were obtained by using {sup 15}N-{sup 1}H heteronuclear three-dimensional (3D) NMR spectroscopy on a uniformly nitrogen-15 enriched sample of the protein, pH 6.6, at 30C. 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 that presence of several helices. Several {sup 15}N and {sup 1}H resonances of the flavin mononucleotide (FMN) prosthetic group have been assigned. The FMN-binding site has been investigated by using polypeptide-FMN NOE's.

OSTI ID:
5602898
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 30:31; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English