处于过渡态类似物形式的42 kDa酶精氨酸激酶的主链共振归属。
Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form.
作者信息
Davulcu Omar, Niu Xiaogang, Brüschweiler-Li Lei, Brüschweiler Rafael, Skalicky Jack J, Chapman Michael S
机构信息
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, 3181 S.W. Sam Jackson Park Road, Portland, OR, 97239-3098, USA.
出版信息
Biomol NMR Assign. 2014 Oct;8(2):335-8. doi: 10.1007/s12104-013-9512-4. Epub 2013 Jul 29.
Abstract
Nearly complete backbone resonance assignments for the 357 residue, 42 kDa enzyme arginine kinase in a transition state analogue (TSA) complex are presented. The TSA is a quaternary complex of arginine kinase, MgADP, arginine, and nitrate. About 93% (320 of 344) of the non-proline backbone amides were assigned using an enzyme enriched with (2)H, (13)C, and (15)N in combination with three enzyme samples prepared with a single (15)N-labeled amino acid (K, L, and R). The amide assignments will provide the foundation for investigating the dynamics of arginine kinase when in a TSA complex.
摘要
本文报道了处于过渡态类似物（TSA）复合物中的357个残基、42 kDa的精氨酸激酶几乎完整的主链共振归属。TSA是精氨酸激酶、MgADP、精氨酸和硝酸盐的四元复合物。使用富含（2）H、（13）C和（15）N的酶，并结合用单一（15）N标记氨基酸（K、L和R）制备的三个酶样品，对约93%（344个中的320个）非脯氨酸主链酰胺进行了归属。酰胺归属将为研究精氨酸激酶处于TSA复合物时的动力学提供基础。
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