tailieunhanh - Báo cáo khoa học: X-ray crystallographic and NMR studies of pantothenate synthetase provide insights into the mechanism of homotropic inhibition by pantoate

The structural basis for the homotropic inhibition of pantothenate synthe-tase by the substrate pantoate was investigated by X-ray crystallography and high-resolution NMR spectroscopic methods. The tertiary structure of the dimeric N-terminal domain of Escherichia colipantothenate synthetase, determined by X-ray crystallography to a resolution of A˚ , showed a second molecule of pantoate bound in the ATP-binding pocket. | ỊFEBS Journal X-ray crystallographic and NMR studies of pantothenate synthetase provide insights into the mechanism of homotropic inhibition by pantoate Kalyan Sundar Chakrabarti Krishan Gopal Thakur B. Gopal and Siddhartha P. Sarma Molecular Biophysics Unit Indian Institute of Science Bangalore India Keywords competitive inhibition NMR pantothenate biosynthesis substrate binding X-ray crystallography Correspondence S. P. Sarma 207 Molecular Biophysics Unit Indian Institute of Science Bangalore 560012 India Fax 91 80 23600535 Tel 91 80 22932839 E-mail sidd@ Present address Department of Biochemistry and Howard Hughes MedicalInstitute MS009 Brandeis University Waltham MA USA Database The 1HN 15N 13Ca 13Cb and 13C chemical shift values of the dimeric N-terminal domain of Escherichia coli pantothenate synthetase have been deposited in BioMagResBank http . under the accession number 6940 The structure factor file and the atomic coordinates of the dimeric N-terminal domain of Escherichia coli pantothenate synthetase bound to three molecules of pantoate have been deposited in the Protein Data Bank under the accession number 3GUZ Received 26 July 2009 revised 6 October 2009 accepted 24 November 2009 doi The structural basis for the homotropic inhibition of pantothenate synthetase by the substrate pantoate was investigated by X-ray crystallography and high-resolution NMR spectroscopic methods. The tertiary structure of the dimeric N-terminal domain of Escherichia coli pantothenate synthetase determined by X-ray crystallography to a resolution of A showed a second molecule of pantoate bound in the ATP-binding pocket. Pantoate binding to the ATP-binding site induced large changes in structure mainly for backbone and side chain atoms of residues in the ATP binding HXGH 34-37 motif. Sequence-specific NMR resonance assignments and solution secondary structure of the dimeric N-terminal domain obtained using .

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