Abstract
Less sedimentation and convection in a microgravity environment has become a well-suited condition for growing high quality protein crystals. Thermostable T1 lipase derived from bacterium Geobacillus zalihae has been crystallized using the counter diffusion method under space and earth conditions. Preliminary study using YASARA molecular modeling structure program for both structures showed differences in number of hydrogen bond, ionic interaction, and conformation. The space-grown crystal structure contains more hydrogen bonds as compared with the earth-grown crystal structure. A molecular dynamics simulation study was used to provide insight on the fluctuations and conformational changes of both T1 lipase structures. The analysis of root mean square deviation (RMSD), radius of gyration, and root mean square fluctuation (RMSF) showed that space-grown structure is more stable than the earth-grown structure. Space-structure also showed more hydrogen bonds and ion interactions compared to the earth-grown structure. Further analysis also revealed that the space-grown structure has long-lived interactions, hence it is considered as the more stable structure. This study provides the conformational dynamics of T1 lipase crystal structure grown in space and earth condition.
Highlights
Protein crystallization is vital to the illumination of the three-dimensional structures of enzymes.Understanding these structures in turn allows for better understanding of the mechanisms and Molecules 2017, 22, 1574; doi:10.3390/molecules22101574 www.mdpi.com/journal/moleculesMolecules 2017, 22, 1574 structural functions of proteins
The crystal structure of earth-grown T1 lipase showed a root mean square deviation (RMSD) of 0.2185 Å when superimposed with the space-grown crystal structure (Figure S1)
The crystal structures of T1 lipase derived from the same crystallization method under space and earth condition showed dissimilarity in both hydrogen bond numbers and ion pair interactions
Summary
Protein crystallization is vital to the illumination of the three-dimensional structures of enzymes.Understanding these structures in turn allows for better understanding of the mechanisms and Molecules 2017, 22, 1574; doi:10.3390/molecules22101574 www.mdpi.com/journal/moleculesMolecules 2017, 22, 1574 structural functions of proteins. Protein crystallization is vital to the illumination of the three-dimensional structures of enzymes. The reduction of buoyancy-driven convection and lack of sedimentation under microgravity condition are the ideal for macromolecular crystal growth. These factors provide better conditions for the formation of high quality protein crystals with better internal orders [1]. Crystallization of macromolecules under microgravity conditions has been shown to improve the size, perfection, morphology, and internal order of protein crystals [2]. Such microgravity-grown crystals can be diffracted to a high resolution
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