6KBW
Crystal structure of Tmm from Myroides profundi D25
Summary for 6KBW
| Entry DOI | 10.2210/pdb6kbw/pdb |
| Descriptor | Trimethylamine monooxygenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | flavin-containing monooxygenase, flavoprotein |
| Biological source | Myroides profundi |
| Total number of polymer chains | 2 |
| Total formula weight | 112923.31 |
| Authors | Li, C.Y.,Zhang, Y.Z. (deposition date: 2019-06-26, release date: 2020-07-08, Last modification date: 2023-11-22) |
| Primary citation | Qin, Q.L.,Wang, Z.B.,Su, H.N.,Chen, X.L.,Miao, J.,Wang, X.J.,Li, C.Y.,Zhang, X.Y.,Li, P.Y.,Wang, M.,Fang, J.,Lidbury, I.,Zhang, W.,Zhang, X.H.,Yang, G.P.,Chen, Y.,Zhang, Y.Z. Oxidation of trimethylamine to trimethylamine N-oxide facilitates high hydrostatic pressure tolerance in a generalist bacterial lineage. Sci Adv, 7:-, 2021 Cited by PubMed Abstract: High hydrostatic pressure (HHP) is a characteristic environmental factor of the deep ocean. However, it remains unclear how piezotolerant bacteria adapt to HHP. Here, we identify a two-step metabolic pathway to cope with HHP stress in a piezotolerant bacterium. D25, obtained from a deep-sea sediment, can take up trimethylamine (TMA) through a previously unidentified TMA transporter, TmaT, and oxidize intracellular TMA into trimethylamine -oxide (TMAO) by a TMA monooxygenase, Tmm. The produced TMAO is accumulated in the cell, functioning as a piezolyte, improving both growth and survival at HHP. The function of the TmaT-Tmm pathway was further confirmed by introducing it into and Encoded TmaT-like and Tmm-like sequences extensively exist in marine metagenomes, and other marine Bacteroidetes bacteria containing genes encoding TmaT-like and Tmm-like proteins also have improved HHP tolerance in the presence of TMA, implying the universality of this HHP tolerance strategy in marine Bacteroidetes. PubMed: 33771875DOI: 10.1126/sciadv.abf9941 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.686 Å) |
Structure validation
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