Conformational changes in arginine kinase upon ligand binding seen by small‐angle X‐ray scattering

FEBS Letters

Dumas, Christian¹  Janin, Joël¹ 

[1] Laboratoire de Biologie Physico-Chimique, Bât 433, Université Paris-Sud, 91405 Orsay Cedex, France

关键词: Arginine kinase;    Radius of gyration;    Hinge bending;    X-ray scattering;   

DOI  :  10.1016/0014-5793(83)80132-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Small-angle X-ray scattering is used to study the effects of substrate binding to lobster arginine kinase in solution. We measure the radius of gyration of the enzyme in the absence and in the presence of ligands. We find that the radius of gyration decreases by 1.20 ± 0.25 Å upon binding ADP-Mg and L-arginine to form the ternary complex. The same decrease is also observed upon binding ADP-Mg alone or ATP-Mg. These results indicate a large conformational change consistent with the hinge motion of domains observed in other phosphokinases.

【 授权许可】

Unknown