Lavanya P, Ramaiah Sudha, Anbarasu Anand
Medical & Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India.
J Biol Phys. 2013 Sep;39(4):649-63. doi: 10.1007/s10867-013-9324-x. Epub 2013 Jun 25.
β-Lactamases produced by pathogenic bacteria cleave β-lactam antibiotics and render them ineffective. Understanding the principles that govern the structural stability of β-lactamases requires elucidation of the nature of the interactions that are involved in stabilization. In the present study, we systematically analyze the influence of CH...O interactions on determining the specificity and stability of β-lactamases in relation to environmental preferences. It is interesting to note that all the residues located in the active site of β-lactamases are involved in CH...O interactions. A significant percentage of CH...O interactions have a higher conservation score and short-range interactions are the predominant type of interactions in β-lactamases. These results will be useful in understanding the stability patterns of β-lactamases.
病原菌产生的β-内酰胺酶可裂解β-内酰胺抗生素并使其失效。要理解支配β-内酰胺酶结构稳定性的原理，需要阐明参与稳定性的相互作用的本质。在本研究中，我们系统地分析了C-H…O相互作用对决定β-内酰胺酶与环境偏好相关的特异性和稳定性的影响。值得注意的是，位于β-内酰胺酶活性位点的所有残基都参与了C-H…O相互作用。相当比例的C-H…O相互作用具有较高的保守分数，并且短程相互作用是β-内酰胺酶中主要的相互作用类型。这些结果将有助于理解β-内酰胺酶的稳定性模式。
