2F40

Structure of a Novel Protein from Backbone-Centered NMR Data and NMR-Assisted Structure Prediction

Summary for 2F40

• Entry DOI: 10.2210/pdb2f40/pdb
• Descriptor: hypothetical protein PF1455 (1 entity in total)
• Functional Keywords: protein structure prediction, residual dipolar couplings, pyrococcus furious, simulated annealing, structural genomics, psi, protein structure initiative, southeast collaboratory for structural genomics, secsg, unknown function
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 1
• Total formula weight: 11245.69

Authors

Bansal, S.,Prestegard, J.H.,Southeast Collaboratory for Structural Genomics (SECSG) (deposition date: 2005-11-22, release date: 2005-12-20, Last modification date: 2024-05-01)

Primary citation

Mayer, K.L.,Qu, Y.,Bansal, S.,LeBlond, P.D.,Jenney, F.E.,Brereton, P.S.,Adams, M.W.,Xu, Y.,Prestegard, J.H.
Structure determination of a new protein from backbone-centered NMR data and NMR-assisted structure prediction.
Proteins, 65:480-489, 2006

PubMed Abstract: 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.

PubMed: 16927360
DOI: 10.1002/prot.21119

Experimental method

SOLUTION NMR