Protein Structure Determination from Pseudocontact Shifts Using ROSETTA

JOURNAL OF MOLECULAR BIOLOGY

卷:416

Article

Schmitz, Christophe²  Vernon, Robert¹  Otting, Gottfried³  Baker, David¹  Huber, Thomas³ 

[1] Univ Washington, Dept Biochem, Seattle, WA 98195 USA

[2] Univ Queensland, Sch Chem & Mol Biosci, Brisbane, Qld 4072, Australia

[3] Australian Natl Univ, Res Sch Chem, Canberra, ACT 0200, Australia

关键词: pseudocontact shift;    protein structure determination;    NMR spectroscopy;    PCS-ROSETTA;    lanthanides;   

DOI  :  10.1016/j.jmb.2011.12.056

来源: Elsevier

【 摘 要 】

Paramagnetic metal ions generate pseudocontact shifts (PCSs) in nuclear magnetic resonance spectra that are manifested as easily measurable changes in chemical shifts. Metals can be incorporated into proteins through metal binding tags, and PCS data constitute powerful long-range restraints on the positions of nuclear spins relative to the coordinate system of the magnetic susceptibility anisotropy tensor (Delta chi-tensor) of the metal ion. We show that three-dimensional structures of proteins can reliably be determined using PCS data from a single metal binding site combined with backbone chemical shifts. The program PCS-ROSETTA automatically determines the Delta chi-tensor and metal position from the PCS data during the structure calculations, without any prior knowledge of the protein structure. The program can determine structures accurately for proteins of up to 150 residues, offering a powerful new approach to protein structure determination that relies exclusively on readily measurable backbone chemical shifts and easily discriminates between correctly and incorrectly folded conformations. (C) 2011 Published by Elsevier Ltd.

【 授权许可】

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