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Literature DB >> 35356954

Detergent-free isolation of CYP450-reductase's FMN-binding domain in E. coli lipid-nanodiscs using a charge-free polymer.

Bankala Krishnarjuna¹, Thirupathi Ravula¹, Ayyalusamy Ramamoorthy¹.

Abstract

The membrane-anchored flavin mononucleotide binding domain (FBD) of CYP450 reductase was extracted in E. coli lipid-nanodiscs using charge-free pentyl-inulin polymer. FBD in nanodiscs was found to be conformationally homogenous and enabled high-resolution NMR probing. 31P NMR revealed the polymer's lack of preference for any specific E. coli lipids and identified the lipid-types in nanodiscs.

Entities: Chemical

Mesh：

Substances：

Year: 2022 PMID： 35356954 PMCID： PMC9578324 DOI： 10.1039/d1cc07193a

Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.065

25 in total

1. Lipids modulate the conformational dynamics of a secondary multidrug transporter.

Authors: Chloé Martens; Richard A Stein; Matthieu Masureel; Aurélie Roth; Smriti Mishra; Rosie Dawaliby; Albert Konijnenberg; Frank Sobott; Cédric Govaerts; Hassane S Mchaourab
Journal: Nat Struct Mol Biol Date: 2016-07-11 Impact factor: 15.369

2. Probing the transmembrane structure and dynamics of microsomal NADPH-cytochrome P450 oxidoreductase by solid-state NMR.

Authors: Rui Huang; Kazutoshi Yamamoto; Meng Zhang; Nataliya Popovych; Ivan Hung; Sang-Choul Im; Zhehong Gan; Lucy Waskell; Ayyalusamy Ramamoorthy
Journal: Biophys J Date: 2014-05-20 Impact factor: 4.033

3. Formation of pH-Resistant Monodispersed Polymer-Lipid Nanodiscs.

Authors: Thirupathi Ravula; Nathaniel Z Hardin; Sudheer Kumar Ramadugu; Sarah J Cox; Ayyalusamy Ramamoorthy
Journal: Angew Chem Int Ed Engl Date: 2018-01-08 Impact factor: 15.336

4. Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes.

Authors: M Wang; D L Roberts; R Paschke; T M Shea; B S Masters; J J Kim
Journal: Proc Natl Acad Sci U S A Date: 1997-08-05 Impact factor: 11.205

5. 1H, 15N and 13C NMR resonance assignment, secondary structure and global fold of the FMN-binding domain of human cytochrome P450 reductase.

Authors: I Barsukov; S Modi; L Y Lian; K H Sze; M J Paine; C R Wolf; G C Roberts
Journal: J Biomol NMR Date: 1997-07 Impact factor: 2.835

Review 1. Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.

Authors: Bankala Krishnarjuna; Ayyalusamy Ramamoorthy
Journal: Biomolecules Date: 2022-08-04

1 in total

Detergent-free isolation of CYP450-reductase's FMN-binding domain in E. coli lipid-nanodiscs using a charge-free polymer.

1. Lipids modulate the conformational dynamics of a secondary multidrug transporter.

2. Probing the transmembrane structure and dynamics of microsomal NADPH-cytochrome P450 oxidoreductase by solid-state NMR.

3. Formation of pH-Resistant Monodispersed Polymer-Lipid Nanodiscs.

4. Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes.

5. 1H, 15N and 13C NMR resonance assignment, secondary structure and global fold of the FMN-binding domain of human cytochrome P450 reductase.

6. Nanodiscs in the studies of membrane-bound cytochrome P450 enzymes.

7. Lipid-exchange in nanodiscs discloses membrane boundaries of cytochrome-P450 reductase.

Review 8. Drugging Membrane Protein Interactions.

Review 9. Nanodiscs: A toolkit for membrane protein science.

Review 10. Membrane protein nanoparticles: the shape of things to come.

Review 1. Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.