Structural and functional investigation of flavin binding center of the NqrC subunit of sodium-translocating NADH:quinone oxidoreductase from Vibrio harveyi

PloS One
Valentin BorshchevskiyValentin Gordeliy

Abstract

Na+-translocating NADH:quinone oxidoreductase (NQR) is a redox-driven sodium pump operating in the respiratory chain of various bacteria, including pathogenic species. The enzyme has a unique set of redox active prosthetic groups, which includes two covalently bound flavin mononucleotide (FMN) residues attached to threonine residues in subunits NqrB and NqrC. The reason of FMN covalent bonding in the subunits has not been established yet. In the current work, binding of free FMN to the apo-form of NqrC from Vibrio harveyi was studied showing very low affinity of NqrC to FMN in the absence of its covalent bonding. To study structural aspects of flavin binding in NqrC, its holo-form was crystallized and its 3D structure was solved at 1.56 Å resolution. It was found that the isoalloxazine moiety of the FMN residue is buried in a hydrophobic cavity and that its pyrimidine ring is squeezed between hydrophobic amino acid residues while its benzene ring is extended from the protein surroundings. This structure of the flavin-binding pocket appears to provide flexibility of the benzene ring, which can help the FMN residue to take the bended conformation and thus to stabilize the one-electron reduced form of the prosthetic group. These p...Continue Reading

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Citations

Aug 5, 2016·Biochemistry·Brian J BenderRocco Moretti
Dec 14, 2019·FEMS Microbiology Letters·Yulia V BertsovaAlexander V Bogachev
Aug 30, 2018·Biochemical Society Transactions·Alexander V BogachevYulia V Bertsova
Oct 28, 2020·FEMS Microbiology Letters·Yulia V BertsovaAlexander V Bogachev
Jul 27, 2021·Bioconjugate Chemistry·Yapei TongMarco W Fraaije

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Methods Mentioned

BETA
Fluorescence
isothermal titration calorimetry
X-ray

Software Mentioned

XDS
MOLREP
MicroCal Origin
DALI
PHENIX

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