1H, 13C and 15N resonance assignments of the apo and holo states of flavodoxin YqcA from Escherichia coli

被引：0
作者：
Ye, Qian [1 ,2 ]
Hu, Yunfei [1 ,3 ]
Jin, Changwen [1 ,2 ,3 ]
机构：
[1] Peking Univ, Beijing Nucl Magnet Resonance Ctr, Beijing 100871, Peoples R China
[2] Peking Univ, Coll Life Sci, Beijing 100871, Peoples R China
[3] Peking Univ, Coll Chem & Mol Engn, Beijing 100871, Peoples R China
来源：
BIOMOLECULAR NMR ASSIGNMENTS | 2014年 / 8卷 / 02期
基金：
中国国家自然科学基金;
关键词：
Flavodoxin; YqcA; Assignments; NMR; DIFFERENTIATING LOOP; BINDING; REDUCTASE; PROTEINS; DYNAMICS; LONG;
D O I：
10.1007/s12104-013-9498-y
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
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 H-1, C-13 and N-15 atoms of E. coli YqcA in both the apo and holo states.
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收藏
页码：269 / 273
页数：5
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