Protein Interactions and Interfaces
EMSL Project ID
19837
Abstract
All proteins interact with other molecules: ligands, metals, membranes, surfaces or other proteins. Such interactions are intrinsic to protein function. We propose to leverage our successful program in Structural Genomics (Northeast Structural Genomics Consortium, NESGC), which has used EMSL NMR instrumentation extensively in the last 6 years, to address protein interactions and interfaces. We will examine three types of interfaces using high resolution liquid state NMR spectroscopy: protein-ligand intefaces, protein-metal interfaces in metalloproteins, and protein-protein interfaces in homo- and hetero-dimeric proteins. We have previously demonstrated our ability to derive atomic-resolution structural information about such interfaces within the context of our Structural Genomics project. We propose to expand our efforts in this direction. Proteins from organisms important in the environment will be selected when possible; for example the NESGC has among the many genomes from which targets are selected the metal reducing bacterium Shewanella oneidensis, and the versatile phototrophic bacterium Rhodopsuedomonas palustris, both of which are of interest to DOE.
Project Details
Project type
Large-Scale EMSL Research
Start Date
2006-08-08
End Date
2009-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
Solution NMR structure of the plasmid-encoded fimbriae regulatory protein PefI fromSalmonella entericaserovar Typhimurium
Aramini JM, P Rossi, JR Cort, LC Ma, R Xiao, T Acton, and G Montelione. 2010. "Solution NMR structure of the plasmid-encoded fimbriae regulatory protein PefI from Salmonella enterica serovar Typhimurium." Proteins. Structure, Function, and Bioinformatics 79(1):335-339. doi:10.1002/prot.22869