5xm3

Publication Abstract from PubMed

The first crystal structure of a pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenase (MDH) from a marine methylotrophic bacterium, Methylophaga aminisulfidivorans MP(T) (MDHMas), was determined at 1.7 A resolution. The active form of MDHMas (or MDHIMas) is a heterotetrameric alpha2beta2, where each beta-subunit assembles on one side of each of the alpha-subunits, in a symmetrical fashion, so that two beta-subunits surround the two PQQ-binding pockets on the alpha-subunits. The active site consists of a PQQ molecule surrounded by a beta-propeller fold for each alpha-subunit. Interestingly, the PQQ molecules are coordinated by a Mg(2+) ion, instead of the Ca(2+) 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 beta-subunits with the alpha-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.

The crystal structure of methanol dehydrogenase, a quinoprotein from the marine methylotrophic bacterium Methylophaga aminisulfidivorans MP(T).,Cao TP, Choi JM, Kim SW, Lee SH J Microbiol. 2018 Feb 28. pii: 10.1007/s12275-018-7483-y. doi:, 10.1007/s12275-018-7483-y. PMID:29492864^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.