Identifying the Underlying Mechanism of G5 Domain Interactions
EMSL Project ID
48617
Abstract
Despite the remarkable success in employing biofilms for a wide range of applications such as the industrial treatment of wastewater and the potential for utilizing biofilms for biofules, exactly how biofilms form and how they are maintained remains poorly understood. For example, biofilm reactors rely on smoothly covered surfaces with detachment and particulate formation leading to potential problems. Thus, a fundamental understanding of microbial adhesion at the molecular level is needed in order to optimize biofilms for their particular applications. To this end, genomic and proteomic methods have identified candidates that may mediate cellular adhesion either through cell-cell interactions that induce biofilm growth or direct interactions with the extracellular polymeric substance (EPS), which comprises a complex mixture of polysaccharides, proteins, and other secreted molecules. A prime example is the “G5 domain” that is present from 1-7 copies within many genes in each bacterial genome and is thought to interact with oligosaccharides and metals. Initially named after 5 glycine residues that are not strictly conserved, these cell-surface exposed G5 domains may both aid in targeting attached enzymes to specific locations as well as mediate cell-cell interactions. However, despite the structural elucidation of several G5 domains to date, their particular interactions remain largely unknown. Here, we will fully characterize several bacterial G5 domains (i.e., structure, dynamics) and then utilize methods to both identify and characterize their interactions. Such a study will significantly contribute to our understanding of the adhesive properties of G5 domains and potentially biofilms in general. For example, by identifying specific interactions of these cell surface proteins here we may be able to exploit a library of interactions to genetically modify biofilms for selective adhesive properties in the future.
Project Details
Project type
Exploratory Research
Start Date
2014-11-11
End Date
2015-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Related Publications
Holliday M, C Camilloni, GS Armstrong, NG Isern, F Zhang, M Vendruscolo, and EZ Eisenmesser. 2015. "Structure and dynamics of GeoCyp: a thermophilic cyclophilin with a novel substrate binding mechanism that functions efficiently at low temperatures." Biochemistry. doi:10.1021/acs.biochem.5b00263