5IQ4

Crystal structure of RnTmm mutant Y207S soaking

Summary for 5IQ4

• Entry DOI: 10.2210/pdb5iq4/pdb
• Related: 5IPY 5IQ1
• Descriptor: Flavin-containing monooxygenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: flavin-containing monooxygenase, flavoprotein
• Biological source: Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM)
• Total number of polymer chains: 2
• Total formula weight: 106635.18

Authors

Zhang, Y.Z.,Li, C.Y. (deposition date: 2016-03-10, release date: 2017-01-18, Last modification date: 2023-11-08)

Primary citation

Li, C.Y.,Chen, X.L.,Zhang, D.,Wang, P.,Sheng, Q.,Peng, M.,Xie, B.B.,Qin, Q.L.,Li, P.Y.,Zhang, X.Y.,Su, H.N.,Song, X.Y.,Shi, M.,Zhou, B.C.,Xun, L.Y.,Chen, Y.,Zhang, Y.Z.
Structural mechanism for bacterial oxidation of oceanic trimethylamine into trimethylamine N-oxide
Mol. Microbiol., 103:992-1003, 2017

PubMed Abstract: Trimethylamine (TMA) and trimethylamine N-oxide (TMAO) are widespread in the ocean and are important nitrogen source for bacteria. TMA monooxygenase (Tmm), a bacterial flavin-containing monooxygenase (FMO), is found widespread in marine bacteria and is responsible for converting TMA to TMAO. However, the molecular mechanism of TMA oxygenation by Tmm has not been explained. Here, we determined the crystal structures of two reaction intermediates of a marine bacterial Tmm (RnTmm) and elucidated the catalytic mechanism of TMA oxidation by RnTmm. The catalytic process of Tmm consists of a reductive half-reaction and an oxidative half-reaction. In the reductive half-reaction, FAD is reduced and a C4a-hydroperoxyflavin intermediate forms. In the oxidative half-reaction, this intermediate attracts TMA through electronic interactions. After TMA binding, NADP bends and interacts with D317, shutting off the entrance to create a protected micro-environment for catalysis and exposing C4a-hydroperoxyflavin to TMA for oxidation. Sequence analysis suggests that the proposed catalytic mechanism is common for bacterial Tmms. These findings reveal the catalytic process of TMA oxidation by marine bacterial Tmm and first show that NADP undergoes a conformational change in the oxidative half-reaction of FMOs.

PubMed: 27997715
DOI: 10.1111/mmi.13605

Experimental method

X-RAY DIFFRACTION (1.5 Å)