Induced Fit in Protein Multimerization: The HFBI Case

Riccardi, Laura; Mereghetti, Paolo

doi:10.1371/journal.pcbi.1005202

Cited by 4 publications

(1 citation statement)

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“…MD simulations were already successfully used previously to study water permeation across lipid mem-branes, 48 aquaporins, 49,50 and other nanopores. 51 Furthermore, MD simulations were used to study class II hydrophobins within solution 52 and at interfaces. 35,53,54 MD Simulations of HFBI Monolayers at the Air− Water Interface Are Stable.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Hydrophobin Bilayer as Water Impermeable Protein Membrane

Nolle,

Starke,

Griffo

et al. 2023

Langmuir

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One of the most important properties of membranes is their permeability to water and other small molecules. A targeted change in permeability allows the passage of molecules to be controlled. Vesicles made of membranes with low water permeability are preferable for drug delivery, for example, because they are more stable and maintain the drug concentration inside. This study reports on the very low water permeability of pure protein membranes composed of a bilayer of the amphiphilic protein hydrophobin HFBI. Using a droplet interface bilayer setup, we demonstrate that HFBI bilayers are essentially impermeable to water. HFBI bilayers withstand far larger osmotic pressures than lipid membranes. Only by disturbing the packing of the proteins in the HFBI bilayer is a measurable water permeability induced. To investigate possible molecular mechanisms causing the near-zero permeability, we used all-atom molecular dynamics simulations of various HFBI bilayer models. The simulations suggest that the experimental HFBI bilayer permeability is compatible neither with a lateral honeycomb structure, as found for HFBI monolayers, nor with a residual oil layer within the bilayer or with a disordered lateral packing similar to the packing in lipid bilayers. These results suggest that the low permeabilities of HFBI and lipid bilayers rely on different mechanisms. With their extremely low but adaptable permeability and high stability, HFBI membranes could be used as an osmotic pressure-insensitive barrier in situations where lipid membranes fail such as desalination membranes.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Hydrophobin Bilayer as Water Impermeable Protein Membrane

Nolle,

Starke,

Griffo

et al. 2023

Langmuir

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Conformational dynamics play important roles upon the function of N-acetylglutamate kinase

Yang

2017

Appl Microbiol Biotechnol

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N-acetylglutamate kinase (NAGK) catalyzes the phosphorylation of N-acetylglutamate. In many bacteria, NAGK catalysis is the rate controlling step in the L-arginine biosynthesis pathway from glutamate to L-arginine and is allosterically inhibited by L-arginine. Many data show that conformational dynamics of NAGKs are essential for their function. The demonstration of the conformational mechanism provides a potential way to improve the yield of arginine. Due to the lack of NAGK catalysis step in arginine synthesis route of mammals, the elucidation of the dynamic mechanism can also provide a way to design a new antivirus drug. This paper reviews how the dynamics affect the activity of NAGKs and are controlled by the effectors. X-ray crystallography and modeling data have shown that in NAGKs, the structural elements required for inhibitor and substrate binding, catalysis and product release, are highly mobile. It is possible to eliminate the inhibition of the arginine and/or block the synthesis of arginine by disturbing the flexibility of the NAGKs. Amino acid kinase family is thought to share some common dynamic features; the flexible structural elements of NAGKs have been identified, but the details of the dynamics and the signal transfer pathways are yet to be elucidated.

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