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Related Concept Videos

Energy to Drive Translocation01:37

Energy to Drive Translocation

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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Structure of Porins01:21

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Mechanical Protein Functions01:58

Mechanical Protein Functions

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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
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  11. The Role Of Protonation In The Pfmate Transporter Protein Structural Transitions

The Role of Protonation in the PfMATE Transporter Protein Structural Transitions

Md Lokman Hossen1, Nisha Bhattarai1, Prem P Chapagain2

  • 1Department of Physics, Florida International University, Miami, FL, USA.

Methods in Molecular Biology (Clifton, N.J.)
|November 14, 2024

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Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
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Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

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Isotopic Effect in Double Proton Transfer Process of Porphycene Investigated by Enhanced QM/MM Method
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View abstract on PubMed

Summary
This summary is machine-generated.

Protonation triggers structural changes in multi-antimicrobial extrusion (MATE) transporters, enabling them to switch between outward-facing and inward-facing states. This mechanism regulates how these membrane proteins expel compounds from cells.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Transport

Background:

  • Multi-antimicrobial extrusion (MATE) transporters are membrane proteins crucial for cellular defense against drugs and toxins.
  • These transporters function by expelling compounds from cells, exhibiting a V-shaped structure that alternates between outward-facing (OF) and inward-facing (IF) conformations to regulate activity.

Purpose of the Study:

  • To computationally investigate the mechanism by which protonation of specific amino acids induces conformational changes in the Pyrococcus furiosus MATE (PfMATE) transporter.
  • To elucidate how these protonation-induced changes facilitate the transition between IF and OF states, regulating PfMATE's antiporter function.

Main Methods:

  • Utilized molecular dynamics (MD) and targeted molecular dynamics (TMD) simulations to study four systems of IF and OF PfMATE within an archaeal lipid bilayer.
Keywords:
Archaeal membranesDynamical network analysisMolecular dynamicsPfMATE

Related Experiment Videos

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

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  • Analyzed hydrogen bond dynamics, potential of mean force, dynamic network analysis, and transfer entropy to understand protonation effects.

    • Main Results:

    • Identified cascading structural changes triggered by protonation at experimentally determined sites within PfMATE.
    • Observed occluded conformations during TMD simulations, providing insights into the transport mechanism.
    • Characterized the role of protonation in driving the conformational switch between IF and OF states.

    Conclusions:

    • Protonation is a key regulator of PfMATE conformational dynamics, driving the transition between inward-facing and outward-facing states.
    • The findings provide a detailed molecular understanding of MATE transporter regulation and antiporter function.
    Potential of mean force
    Protonation
    Structural transition
    Transfer entropy