Solution NMR-derived Global Fold of a Monomeric 82 kDa Enzyme

Vitali Tugarinov, University of Toronto
Wing-Yiu Choy, University of Toronto
Vladislav Yu Orekhov, Goteborg University
Lewis E. Kay, University of Toronto

Published in: PNAS January 18, 2005 vol. 102 no. 3 622-627. doi: 10.1073/pnas.0407792102 Dr. Wing-Yiu Choy is currently a faculty member at The University of Western Ontario.

Abstract

The size of proteins that can be studied by solution NMR spectroscopy has increased significantly because of recent developments in methodology. Important experiments include those that make use of approaches that increase the lifetimes of NMR signals or that define the orientation of internuclear bond vectors with respect to a common molecular frame. The advances in NMR techniques are strongly coupled to isotope labeling methods that increase sensitivity and reduce the complexity of NMR spectra. We show that these developments can be exploited in structural studies of highmolecular- weight, single-polypeptide proteins, and we present the solution global fold of the monomeric 723-residue (82-kDa) enzyme malate synthase G from Escherichia coli, which has been extensively characterized by NMR in the past several years.