5XM3
Crystal Structure of Methanol dehydrogenase from Methylophaga aminisulfidivorans
5XM3 の概要
| エントリーDOI | 10.2210/pdb5xm3/pdb |
| 分子名称 | Glucose dehydrogenase, Methanol dehydrogenase [cytochrome c] subunit 2, PYRROLOQUINOLINE QUINONE, ... (5 entities in total) |
| 機能のキーワード | marine, methanol dehydrogenase, methylophaga, pyrroloquinoline quinone, mg++, oxidoreductase |
| 由来する生物種 | Methylophaga aminisulfidivorans MP 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 159350.10 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 29492864DOI: 10.1007/s12275-018-7483-y 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.701 Å) |
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