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目的:探讨金属β-内酰胺酶残基在结构上的变化程度。方法:对各亚类MBLs结构进行叠合,计算残基间RMSD值,根据RMSD值差异引入基于结构的香农熵,并将基于结构的香农熵映射到1DD6结构上。结果:结构上的变化主要集中在活性位点附近靠外的区域,而活性位点内部则相对变化较小。结论:在活性位点附近loop区残基结构在不同MBLs中变化较大,是决定各亚类MBLs水解活性和特异性的主要因素。这一发现对于指导计算机辅助MBLs抑制剂的设计有着重要的指导作用。
Objective: To investigate the structural changes of metal β-lactamase residues. Methods: The sub-classes of MBLs were stacked and the RMSD values were calculated. Based on the difference of RMSD values, structure-based Shannon entropy was introduced and structure-based Shannon entropy was mapped to 1DD6 structure. Results: The structural changes mainly concentrated in the outer area near the active site, while the relative changes in the active site were relatively small. CONCLUSION: The residues in the loop region near the active site vary greatly in different MBLs and are the major factors that determine the activity and specificity of MBLs in each subtype. This finding is of great importance in guiding the design of computer-aided MBL inhibitors.