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

Overview

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.

About this Structure

2F40 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

Structure determination of a new protein from backbone-centered NMR data and NMR-assisted structure prediction., Mayer KL, Qu Y, Bansal S, LeBlond PD, Jenney FE Jr, Brereton PS, Adams MW, Xu Y, Prestegard JH, Proteins. 2006 Nov 1;65(2):480-9. PMID:16927360

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