Department of Genetics, Development and Cell Biology, Iowa State University, Ames, IA 50011, USA.
J Biomol Struct Dyn. 2011 Dec;29(3):509-26. doi: 10.1080/07391102.2011.10507402.
Thermostable endoglucanases play a crucial role in the production of biofuels to breakdown plant cellulose. Analyzing their structure-dynamics relationship can inform about the origins of their thermostability. Although tertiary structures of many endoglucanase proteins are available, the relationship between thermostability, structure, and dynamics is not explored fully. We have generated elastic network models for thermostable and mesostable endoglucanases with the (αβ)₈ fold in substrate bound and unbound states. The comparative analyses shed light on the relation between protein dynamics, thermostability, and substrate binding. We observed specific differences in the dynamic behavior of catalytic residues in slow modes: while both the nucleophile and the acid/base donor residues show positively correlated motions in the thermophile, their dynamics is uncoupled in the mesophile. Our proof-of-concept comparison study suggests that global dynamics can be harnessed to further our understanding of thermostability.
热稳定性内切葡聚糖酶在生物燃料生产中起着至关重要的作用，可以分解植物纤维素。分析它们的结构-动力学关系可以了解其热稳定性的起源。尽管许多内切葡聚糖酶蛋白的三级结构已经可用，但热稳定性、结构和动力学之间的关系尚未得到充分探索。我们已经为结合和未结合状态下具有（αβ）₈折叠的热稳定和中稳定内切葡聚糖酶生成了弹性网络模型。比较分析揭示了蛋白质动力学、热稳定性和底物结合之间的关系。我们观察到在慢模式下催化残基的动态行为存在特定差异：虽然亲核试剂和酸/碱供体残基在嗜热菌中都表现出正相关运动，但在中温菌中它们的动力学是解耦的。我们的概念验证比较研究表明，可以利用整体动力学来进一步了解热稳定性。
