1Y8B

Solution NMR-Derived Global Fold of Malate Synthase G from E.coli

Summary for 1Y8B

• Entry DOI: 10.2210/pdb1y8b/pdb
• Related: 1D8C 1P7T
• Descriptor: Malate synthase G (1 entity in total)
• Functional Keywords: nmr global fold, apo-malate synthase g, 82 kda enzyme, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P37330
• Total number of polymer chains: 1
• Total formula weight: 81636.52

Authors

Tugarinov, V.,Choy, W.-Y.,Orekhov, V.Y.,Kay, L.E. (deposition date: 2004-12-10, release date: 2005-01-11, Last modification date: 2024-05-22)

Primary citation

Tugarinov, V.,Choy, W.-Y.,Orekhov, V.Y.,Kay, L.E.
Solution NMR-derived global fold of a monomeric 82-kDa enzyme.
Proc.Natl.Acad.Sci.USA, 102:622-627, 2005

PubMed 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 high-molecular-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.

PubMed: 15637152
DOI: 10.1073/pnas.0407792102

Experimental method

SOLUTION NMR