title: ¹H, ¹³C and ¹⁵N resonance assignments of the apo and holo states of flavodoxin YqcA from Escherichia coli.
abstract: Flavodoxins are a family of FMN binding proteins widely distributed in prokaryotes. They involve in various electron transfer reactions using the non-covalently bound FMN cofactor as the redox center. The Escherichia coli yqcA gene was identified to encode a short-chain favodoxin based on sequence information. However, the structure of YqcA protein is unknown and its exact biological function in cell is yet to be investigated. Herein, we report the resonance assignments of (1)H, (13)C and (15)N atoms of E. coli YqcA in both the apo and holo states.
authors.affiliation: Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing, 100871, China.
authors.forename: Qian
authors.initials: Q
authors.lastname: Ye
authors.forename: Yunfei
authors.initials: Y
authors.lastname: Hu
authors.forename: Changwen
authors.initials: C
authors.lastname: Jin
mesh_terms: D001059:Apoproteins / Q000737:chemistry*; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry*; D005418:Flavodoxin / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular
chemical_list: D001059:Apoproteins; D029968:Escherichia coli Proteins; D005418:Flavodoxin