Crystallization and initial X-ray diffraction analysis of the tellurite-resistance S-adenosyl-L-methionine transferase protein TehB from Escherichia coli.
TehB is an S-adenosyl-L-methionine (SAM) dependent methyltransferase that detoxifies tellurite in bacteria. The Escherichia coli TehB protein was purified and crystallized in the presence of both SAM and sinefungin. The TehB-SAM and TehB-sinefungin crystals both diffracted X-rays to 1.9 Å resolution. The TehB-SAM crystals belonged to space group C2, with unit-cell parameters a = 60.0, b = 56.1, c = 130.6 Å, β = 97.9°. The TehB-sinefungin crystals belonged to space group P2(1), with unit-cell parameters a = 59.1, b = 55.5, c = 129.7 Å, β = 95.9°.
Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Chilton, Oxfordshire OX11 0DE, England.
Hassanul Ghani
HG
Choudhury
Konstantinos
K
Beis
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008780:Methyltransferases / Q000737:chemistry*; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D029968:Escherichia coli Proteins; C119920:tellurite resistance protein B, E coli; D008780:Methyltransferases; C093871:methionine S-methyltransferase