Location of divalent ion sites in acyl carrier protein using relaxation perturbed 2D NMR

FEBS Letters

Prestegard, James H.²  Frederick, Anne F.¹  Kay, Lewis E.² 

[1] Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA;Department of Chemistry, Yale University, New Haven, CT 06511 USA

关键词: 2D NMR;    Mn2+;    Acyl carrier protein;    Spin-lattice relaxation rate;    AMBER;    2D;    two-dimensional;    ACP;    acyl carrier protein;    NOE;    nuclear Overhauser effect;    T 1;    spin-lattice relaxation rate;    T 2;    spin-spin relaxation rate;    COSY;    coupling correlated spectroscopy;    DTT;    dithiothreitol;    RMS;    root mean square;    AMBER;    Assisted Model Building with Energy Refinement;    a program licensed from the Regents of the University of California;    Copyright 1986;    UCSF;   

DOI  :  10.1016/0014-5793(88)80222-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The T ₁-accordion COSY experiment has been applied to acyl carrier protein (ACP) to locate the divalent ion binding sites in the protein using the paramagnetic ion, Mn²⁺, as a substitute for Ca²⁺. Replacement with Mn²⁺ leads to an enhancement of proton spin-lattice (T ₁) relaxation rates. These enhancements have a l/r ⁶, distance dependence that makes them extremely useful in structural analyses. Ion-proton distances ranging from 3.0 to 9.0 Å have been obtained from this experiment and subsequently used as constraints in the molecular mechanics module of AMBER to refine a protein structure.

【 授权许可】

Unknown