Protein Structure Determination from Pseudocontact Shifts Using ROSETTA

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• 作者：Christophe Schmitz¹ ; ¹ ; ^&dagger ; ; ^{C.P.F.Schmitz@uu.nl} ; Robert Vernon² ; ^&dagger ; ; ^{rvernon@u.washington.edu} ; Gottfried Otting³ ; ^{go@rsc.anu.edu.au} ; David Baker² ; ^{dabaker@u.washington.edu} ; Thomas Huber³ ; ^{t.huber@uq.edu.au}
• 关键词：PCS ; pseudocontact shift ; 3D ; three-dimensional ; NOE ; nuclear Overhauser enhancement
• 刊名：Journal of Molecular Biology
• 出版年：2012
• 期刊代码：102_00222836
• 类别：imm
• 出版时间：9 March, 2012
• 卷：416
• 期：5
• 页码：668-677
• 文件大小：1056 K

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 (螖蠂-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 螖蠂-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.