Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AM1

被引:31
作者
Labesse, I
Ferrari, D
Chen, ZW
Rossi, GL
Kuusk, V
McIntire, WS
Mathews, FS [1 ]
机构
[1] Washington Univ, Sch Med, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA
[2] Dept Vet Affairs Med Ctr, Div Mol Biol, San Francisco, CA 94121 USA
[3] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA
[4] Univ Calif San Francisco, Dept Anesthesia, San Francisco, CA 94143 USA
[5] Univ Parma, Ist Sci Biochim, I-43100 Parma, Italy
关键词
D O I
10.1074/jbc.273.40.25703
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Various monovalent cations influence the enzymatic activity and the spectroscopic properties of methylamine dehydrogenase (MADH). Here, we report the structure determination of this tryptophan tryptophylquinone-containing enzyme from Methylobacterium extorquens AM1 by high resolution x-ray crystallography (1.75 Angstrom). This first MADH crystal structure at low ionic strength is compared with the high resolution structure of the related MADH from Paracoccus denitrificans recently reported. We also describe the first structures (at 1.95 to 2.15 Angstrom resolution) of an MADH in the substrate-reduced form and in the presence of trimethylamine and of cesium, two competitive inhibitors. Polarized absorption microspectrophotometry was performed on single crystals under various redox, pH, and salt conditions. The results show that the enzyme is catalytically active in the crystal and that the cations cause the same spectral perturbations as are observed in solution. These studies lead us to propose a model for the entrance and binding of the substrate in the active site.
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收藏
页码:25703 / 25712
页数:10
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