¹H, ¹³C and ¹âµN resonance assignments of the apo and holo states of flavodoxin YqcA from Escherichia coli.
Biomol NMR Assign. 2014 Oct;8(2):269-73. doi:10.1007/s12104-013-9498-y. Epub 2013 Jun 09
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摘要
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.
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原始数据
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文献解读
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