Structure determination of a new protein from backbone-centered NMR data and NMR-assisted structure prediction
Targeting of proteins for structure determination in structural genomic programs often includes the use of threading and fold recognition methods to exclude proteins belonging to well-populated fold families, but such methods can still fail to recognize preexisting folds. The authors illustrate here a method in which limited amounts of structural data are used to improve an initial homology search and the data are subsequently used to produce a structure by data-constrained refinement of an identified structural template. The data used are primarily NMR-based residual dipolar couplings, but they also include additional chemical shift and backbone-nuclear Overhauser effect data. Using this methodology, a backbone structure was efficiently produced for a 10 kDa protein (PF1455) from Pyrococcus furiosus. Its relationship to existing structures and its probable function are discussed. Â© 2006 Wiley-Liss, Inc.
Proteins: Structure, Function and Genetics
Mayer, K. L.; Qu, Y.; Bansal, S.; Leblond, P. D.; Jenney, Francis E. Jr.; Brereton, P. S.; Adams, M. W.; Xu, Y.; and Prestegard, J. H., "Structure determination of a new protein from backbone-centered NMR data and NMR-assisted structure prediction" (2006). PCOM Scholarly Papers. 599.