title: Dynamics of endoglucanase catalytic domains: implications towards thermostability.
abstract: 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.
authors: Department of Genetics, Development and Cell Biology, Iowa State University, Ames, IA 50011, USA.
authors: Ragothaman M
authors: RM
authors: Yennamalli
authors: Jeffrey D
authors: JD
authors: Wolt
authors: Taner Z
authors: TZ
authors: Sen
mesh_terms: D001407:Bacillus / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D020134:Catalytic Domain; D002480:Cellulase / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D017510:Protein Folding; D055550:Protein Stability; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D002480:Cellulase