利用激光极化129Xe核磁共振区分多种趋化性Y蛋白构象。
Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR.
作者信息
Lowery Thomas J, Doucleff Michaeleen, Ruiz E Janette, Rubin Seth M, Pines Alexander, Wemmer David E
机构信息
Physical Biosciences Divisions, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.
出版信息
Protein Sci. 2005 Apr;14(4):848-55. doi: 10.1110/ps.041231005. Epub 2005 Mar 1.
Abstract
The chemical shift of the (129)Xe NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins. Here we show that the (129)Xe shift can sense more subtle changes: magnesium binding, BeF(3)(-) activation, and peptide binding by the Escherichia coli chemotaxis Y protein. (1)H-(15)N correlation spectroscopy and X-ray crystallography were used to identify two xenon-binding cavities in CheY that are primarily responsible for the shift changes. One site is near the active site, and the other is near the peptide binding site.
摘要
已证明¹²⁹Xe核磁共振信号的化学位移对该原子周围的局部环境极为敏感，并已用于追踪诸如细菌周质结合蛋白的配体结合等过程。在此我们表明，¹²⁹Xe位移能够感知更细微的变化：镁离子结合、BeF₃⁻激活以及大肠杆菌趋化性Y蛋白的肽结合。利用¹H-¹⁵N相关光谱和X射线晶体学确定了CheY中两个主要导致位移变化的氙结合腔。一个位点靠近活性位点，另一个位点靠近肽结合位点。
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