1y8b | pdb_00001y8b

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

spinqualitylabelsall models 1y8b, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1y8b is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1d8c, 1p7t Gene: glcB, glc ("Bacillus coli" Migula 1895) Activity: Malate synthase, with EC number 2.3.3.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Warning: this is a large structure, and loading might take a long time or not happen at all. Function [MASZ_ECOLI] Accounts for almost the entire malate-synthesizing activity in cells metabolizing glyoxylate.[HAMAP-Rule:MF_00641] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Solution NMR-derived global fold of a monomeric 82-kDa enzyme.,Tugarinov V, Choy WY, Orekhov VY, Kay LE Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):622-7. Epub 2005 Jan 6. PMID:15637152 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Malate synthase

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