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首页> 外文期刊>Biochemistry >Identification of the binding surface on beta-lactamase for GroEL by limited proteolysis and MALDI mass spectrometry
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Identification of the binding surface on beta-lactamase for GroEL by limited proteolysis and MALDI mass spectrometry

机译：通过有限的蛋白水解和MALDI质谱鉴定β-内酰胺酶对GroEL的结合表面

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Escherichia coli beta-lactamase, alone or as a complex with GroEL at 48 degrees C, was partially digested with trypsin, endoproteinase Glu-C, or thermolysin. Peptides were analyzed by matrix-assisted laser desorption and ionization mass spectrometry and aligned with the known sequence. From the protease cleavage sites which become protected upon binding and those which become newly accessible, a model of the complex is proposed in which the carboxy-terminal helix has melted, two loops form the binding interface and the large beta-sheet become partially uncovered by the slight dislocation of other structural elements. This explains how hydrophobic surface on the substrate protein can become accessible while scarcely disrupting the hydrogen bond network of the native structure. An analysis of the GroEL-bound peptides bound after digestion of the beta-lactamase showed no obvious sequence motifs, indicating that binding is provided by hydrophobic patches in the three-dimensional structure. [References: 59]
机译：大肠杆菌β-内酰胺酶，单独或与GroEL在48摄氏度下形成复合物，可以用胰蛋白酶，内蛋白酶Glu-C或嗜热菌蛋白酶部分消化。通过基质辅助激光解吸和电离质谱分析肽，并与已知序列比对。从结合时受保护的蛋白酶切割位点和新近可进入的那些位点，提出了一种复合物模型，其中羧基末端螺旋已融化，两个环形成了结合界面，大的β-折叠被部分覆盖。其他结构元素的轻微错位。这解释了底物蛋白质上的疏水表面如何变得可访问，而几乎不破坏天然结构的氢键网络。消化β-内酰胺酶后结合的与GroEL结合的肽的分析显示没有明显的序列基序，表明在三维结构中疏水性补丁提供了结合。 [参考：59]

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