Related Experiment Video
Updated: Mar 25, 2026
Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Insights into conformational regulation of PfMATE transporter from Pyrococcus furiosus induced by alternating
Xiaojie Jin1, Yonghua Shao1, Qifeng Bai1
1State Key Laboratory of Applied Organic Chemistry, Department of Chemistry, Lanzhou University, Lanzhou 730000, China.
Background:
Multidrug and toxic compound extrusion (MATE) family transporters induce multiple-drug resistance (MDR) of bacterial pathogens and cancer cells, thus causing critical reductions in the therapeutic efficacies of antibiotics and anti-cancer drugs. Unfortunately, to date, the details and intrinsic reason about conformational regulation mechanism of MATE transporters remain elusive.
Method:
In this work, molecular dynamics (MD) simulations were conducted to explore the conformational regulation mechanism of PfMATE transporter from Pyrococcus furiosus based on different protonation state of Asp41. Two (MD) simulation systems were investigated: a system with protonation of Asp41 and a system without protonation of Asp41, which were named by D184(H)D41(H) system and D184(H) system, respectively.
Results And Conclusions:
Firstly, MD simulation results indicate that conformational changes mainly happen in extracellular regions of PfMATE protein. Further analysis reveals that PfMATE protein experiences different motion mode and forms different conformation based on different protonation state of Asp41. In the D184(H)D41(H) system, PfMATE experiences an opening motion and forms a more outward-open conformation. As for the D184(H) system, the protein has an anticlockwise rotational motion with the channel axis of protein and the more outward-open conformation does not appear. It can be inferred that protonation of Asp41 is essential for conformational regulation of PfMATE during transporting substrates.
General Significance:
These findings provide intrinsic information for understanding the conformational regulation mechanism of PfMATE and will be very meaningful to explore the MDR mechanism of PfMATE further.
More Related Videos
06:50Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
Published on: January 26, 2024
12:07Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
Related Concept Videos
01:19Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
02:04Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
01:02Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
00:49Ligand Binding and Linkage