水介导的静电相互作用赋予了来自大肠杆菌的GrpE蛋白“尾部”区域热稳定性。
A water mediated electrostatic interaction gives thermal stability to the "tail" region of the GrpE protein from E. coli.
作者信息
Mehl Andrew F, Demeler Borries, Zraikat Afaq
机构信息
Department of Chemistry, Knox College, Galesburg, IL 61401, USA.
出版信息
Protein J. 2007 Jun;26(4):239-45. doi: 10.1007/s10930-006-9065-9.
Abstract
The GrpE protein from E. coli is a homodimer with an unusual structure of two long paired alpha-helices from each monomer interacting in a parallel arrangement to form a "tail" at the N-terminal end. Using site-directed mutagenesis, we show that there is a key electrostatic interaction involving R57 (mediated by a water molecule) that provides thermal stability to this "tail" region. The R57A mutant showed a drop in T (m) of 8.5 degrees C and a smaller DeltaH (u) (unfolding) compared to wild-type for the first unfolding transition, but no significant decrease in dimer stability as shown through equilibrium analytical ultracentrifugation studies. Another mutant (E94A) at the dimer interface showed a decrease in DeltaH (u )but no drop in T (m) for the second unfolding transition and a slight increase in dimer stability.
摘要
来自大肠杆菌的GrpE蛋白是一种同型二聚体，具有独特的结构，每个单体的两条长的配对α螺旋以平行排列相互作用，在N端形成一个“尾巴”。通过定点诱变，我们发现存在一个涉及R57的关键静电相互作用（由一个水分子介导），它为这个“尾巴”区域提供热稳定性。与野生型相比，R57A突变体在第一次解折叠转变时，T（m）下降了8.5摄氏度，ΔH（u）（解折叠）更小，但通过平衡分析超速离心研究表明二聚体稳定性没有显著下降。二聚体界面处的另一个突变体（E94A）在第二次解折叠转变时，ΔH（u）降低，但T（m）没有下降，并且二聚体稳定性略有增加。
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