Structure of the NPr:EIN<sup>Ntrsup> Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems

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• 作者：Madeleine Strickland<sup>1sup> ; Ann Marie Stanley<sup>2sup> ; Guangshun Wang<sup>3sup> ; Istvan Botos<sup>2sup> ; Charles D. Schwieters<sup>4sup> ; Susan K. Buchanan<sup>2sup> ; Alan Peterkofsky<sup>5sup><sup> ; sup><sup>peterkofsky@nih.govsup> ; Nico Tjandra<sup>1sup><sup> ; sup><sup>6sup><sup> ; sup><sup>tjandran@nhlbi.nih.govsup>
• 关键词：Enzyme I ; phosphotransferase system ; nuclear magnetic resonance ; X-ray crystallography ; small-angle X-ray scattering ; NPr ; residual dipolar couplings ; pseudocontact shifts ; specificity ; surface potential
• 刊名：Structure
• 出版年：2016
• 出版时间：6 December 2016
• 年：2016
• 卷：24
• 期：12
• 页码：2127-2137
• 全文大小：4104 K
• 卷排序：24

文摘

The 28 kDa EINNtr structure was solved by X-ray crystallography Sparse NMR restraints and SAXS were used to dock and refine the NPr:EINNtr complex Residues necessary for enzymatic function (phosphorylation) were identified Specificity of the complexes is a result of a difference in surface potential