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The crystal structure of methanol dehydrogenase, a quinoprotein from the marine methylotrophic bacterium Methylophaga aminisulfidivorans MPT
Thinh-Phat Cao 1, Jin Myung Choi 1, Si Wouk Kim 2, Sung Haeng Lee 1
Journal of Microbiology 2018;56(4):246-254.
DOI: https://doi.org/10.1007/s12275-018-7483-y
Published online: February 28, 2018
1Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju 61452, Republic of Korea, 2Department of Environmental Engineering, Chosun University, Gwangju 61452, Republic of Korea1Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju 61452, Republic of Korea, 2Department of Environmental Engineering, Chosun University, Gwangju 61452, Republic of Korea
Corresponding author:  Sung Haeng Lee , Tel: +82-62-230-6381, 
Received: 7 November 2017   • Revised: 11 January 2018   • Accepted: 15 January 2018
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Abstract

The first crystal structure of a pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenase (MDH) from a marine methylotrophic bacterium, Methylophaga aminisulfidivorans MPT (MDHMas), was determined at 1.7 Å resolution. The active form of MDHMas (or MDHIMas) is a heterotetrameric α2β2, where each β-subunit assembles on one side of each of the α-subunits, in a symmetrical fashion, so that two β-subunits surround the two PQQ-binding pockets on the α-subunits. The active site consists of a PQQ molecule surrounded by a β-propeller fold for each α-subunit. Interestingly, the PQQ molecules are coordinated by a Mg2+ ion, instead of the Ca2+ ion that is commonly found in the terrestrial MDHI, indicating the efficiency of osmotic balance regulation in the high salt environment. The overall interaction of the β-subunits with the α-subunits appears tighter than that of terrestrial homologues, suggesting the efficient maintenance of MDHIMas integrity in the sea water environment to provide a firm basis for complex formation with MxaJMas or Cyt cL. With the help of the features mentioned above, our research may enable the elucidation of the full molecular mechanism of methanol oxidation by taking advantage of marine bacterium-originated proteins in the methanol oxidizing system (mox), including MxaJ, as the attainment of these proteins from terrestrial bacteria for structural studies has not been successful.

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    The crystal structure of methanol dehydrogenase, a quinoprotein from the marine methylotrophic bacterium Methylophaga aminisulfidivorans MPT
    J. Microbiol. 2018;56(4):246-254.   Published online February 28, 2018
    DOI: https://doi.org/10.1007/s12275-018-7483-y
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