Solution Structure and NH Exchange Studies of the MutT Pyrophosphohydrolase Complexed with Mg2+ and 8-Oxo-dGMP, a Tightly Bound Product

Autor:	Hugo F. Azurmendi, Albert S. Mildvan, V. Saraswat, Michael A. Massiah
Rok vydání:	2003
Předmět:	Models Molecular Molecular Sequence Data Guanosine Monophosphate Arginine Biochemistry Protein Structure Secondary Substrate Specificity Adenosine Triphosphate Protein structure Escherichia coli Side chain Magnesium Amino Acid Sequence Pyrophosphatases Binding site Nuclear Magnetic Resonance Biomolecular Binding Sites Chemistry Hydrogen bond Escherichia coli Proteins Deoxyguanine Nucleotides Hydrogen Bonding Phosphoric Monoester Hydrolases Recombinant Proteins Protein tertiary structure Protein Structure Tertiary Solutions Crystallography Heteronuclear molecule Residual dipolar coupling Helix Nucleic Acid Conformation Protein Binding
Zdroj:	Biochemistry. 42:10140-10154
ISSN:	1520-4995 0006-2960
Popis:	To learn the structural basis for the unusually tight binding of 8-oxo-nucleotides to the MutT pyrophosphohydrolase of Escherichia coli (129 residues), the solution structure of the MutT-Mg(2+)-8-oxo-dGMP product complex (K(D) = 52 nM) was determined by standard 3-D heteronuclear NMR methods. Using 1746 NOEs (13.5 NOEs/residue) and 186 phi and psi values derived from backbone (15)N, Calpha, Halpha, and Cbeta chemical shifts, 20 converged structures were computed with NOE violations
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82f5aa2079a9e1734bc7bc17aa45a7fd https://doi.org/10.1021/bi030105p Zobrazit plný text záznamu