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.
Mayer
K L
KL
Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA.
Qu
Y
Y
Bansal
S
S
LeBlond
P D
PD
Jenney
F E
FE
Brereton
P S
PS
Adams
M W W
MW
Xu
Y
Y
Prestegard
J H
JH
D019843:Archaeal Proteins / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D020027:Pyrococcus furiosus / Q000737:chemistry; D040681:Structural Homology, Protein
D019843:Archaeal Proteins