5XM3

Crystal Structure of Methanol dehydrogenase from Methylophaga aminisulfidivorans

Summary for 5XM3

• Entry DOI: 10.2210/pdb5xm3/pdb
• Descriptor: Glucose dehydrogenase, Methanol dehydrogenase [cytochrome c] subunit 2, PYRROLOQUINOLINE QUINONE, ... (5 entities in total)
• Functional Keywords: marine, methanol dehydrogenase, methylophaga, pyrroloquinoline quinone, mg++, oxidoreductase
• Biological source: Methylophaga aminisulfidivorans MP; More
• Total number of polymer chains: 4
• Total formula weight: 159350.10

Authors

Cao, T.P.,Choi, J.M.,Lee, S.H. (deposition date: 2017-05-12, release date: 2018-03-21, Last modification date: 2024-11-20)

Primary citation

Cao, T.P.,Choi, J.M.,Kim, S.W.,Lee, S.H.
The crystal structure of methanol dehydrogenase, a quinoprotein from the marine methylotrophic bacterium Methylophaga aminisulfidivorans MPT
J. Microbiol., 56:246-254, 2018

PubMed Abstract: The first crystal structure of a pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenase (MDH) from a marine methylotrophic bacterium, Methylophaga aminisulfidivorans MP (MDH ), was determined at 1.7 Å resolution. The active form of MDH (or MDHI ) is a heterotetrameric αβ, 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 Mg ion, instead of the Ca 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 MDHI integrity in the sea water environment to provide a firm basis for complex formation with MxaJ or Cyt c. 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.

PubMed: 29492864
DOI: 10.1007/s12275-018-7483-y

Experimental method

X-RAY DIFFRACTION (1.701 Å)