来自枯草芽孢杆菌的组氨酸激酶抑制剂KipI的N端结构域的1H、13C和15N主链及侧链共振归属
1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis.
作者信息
Hynson Robert M G, Kwan Ann H, Jacques David A, Mackay Joel P, Trewhella Jill
机构信息
School of Molecular Biosciences, The University of Sydney, New South Wales, 2006, Australia.
出版信息
Biomol NMR Assign. 2010 Oct;4(2):167-9. doi: 10.1007/s12104-010-9237-6. Epub 2010 Jun 4.
KipI is a sporulation inhibitor in Bacillus subtilis which acts by binding to the dimerisation and histidine phosphotransfer (DHp) domain of KinA, the principle input kinase in the phosphorelay responsible for sporulation. The (15)N, (13)C and (1)H chemical shift assignments of the N-terminal domain of KipI were determined using multidimensional, multinuclear NMR experiments. The N-terminal domain has two conformers and resonance assignments have been made for both conformers.
KipI是枯草芽孢杆菌中的一种芽孢形成抑制剂，它通过与KinA的二聚化和组氨酸磷酸转移（DHp）结构域结合而起作用，KinA是负责芽孢形成的磷酸转移中的主要输入激酶。利用多维多核核磁共振实验确定了KipI N端结构域的（15）N、（13）C和（1）H化学位移归属。N端结构域有两种构象，并且已经对这两种构象进行了共振归属。
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