Articles with "dimer interface" as a keyword



Dynamics of the E. coli β-Clamp Dimer Interface and Its Influence on DNA Loading.

Sign Up to like & get
recommendations!
Published in 2019 at "Biophysical journal"

DOI: 10.1016/j.bpj.2019.06.035

Abstract: The ring-shaped sliding clamp proteins have crucial roles in the regulation of DNA replication, recombination, and repair in all organisms. We previously showed that the Escherichia coli β-clamp is dynamic in solution, transiently visiting conformational… read more here.

Keywords: coli clamp; temperature; dimer interface; dna ... See more keywords

The PHY domain dimer interface of bacteriophytochromes mediates cross-talk between photosensory modules and output domains.

Sign Up to like & get
recommendations!
Published in 2021 at "Journal of molecular biology"

DOI: 10.1016/j.jmb.2021.167092

Abstract: Protein dynamics play a major role for the catalytic function of enzymes, the interaction of protein complexes or signal integration in regulatory proteins. In the context of multi-domain proteins involved in light-regulation of enzymatic effectors,… read more here.

Keywords: phy domain; photosensory; dimer interface; role ... See more keywords

Long-Range Destabilizing Effects of Mutations at the β Clamp Dimer Interface

Sign Up to like & get
recommendations!
Published in 2025 at "Biochemistry"

DOI: 10.1021/acs.biochem.5c00135

Abstract: The bacterial processivity factor, the β sliding clamp, endows Pol III DNA polymerase α with efficiency and processivity during DNA replication by tethering α to DNA. The dimeric β clamp is loaded onto primer:template DNA… read more here.

Keywords: dimer interface; long range; clamp dimer; interface ... See more keywords

Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems.

Sign Up to like & get
recommendations!
Published in 2018 at "Biochemistry"

DOI: 10.1021/acs.biochem.7b01275

Abstract: In the Suf Fe-S cluster assembly pathway, the activity of the cysteine desulfurase, SufS, is regulated by interactions with the accessory sulfotransferase protein, SufE. SufE has been shown to stimulate SufS activity, likely by inducing… read more here.

Keywords: dimer interface; cysteine desulfurase; sufs; mechanism ... See more keywords

Bacterial Analogs to Cholesterol Affect Dimerization of Proteorhodopsin and Modulates Preferred Dimer Interface.

Sign Up to like & get
recommendations!
Published in 2021 at "Journal of chemical theory and computation"

DOI: 10.1021/acs.jctc.0c01174

Abstract: Hopanoids, the bacterial analogues of sterols, are ubiquitous in bacteria and play a significant role in organismal survival under stressful environments. Unlike sterols, hopanoids have a high degree of variation in the size and chemical… read more here.

Keywords: dimerization; proteorhodopsin; dimer interface; affect dimerization ... See more keywords

Aromatic Residue F443 Modulates the Dimer Interface and Activity of Pseudomonas mandelii Glutathione Reductase

Sign Up to like & get
recommendations!
Published in 2025 at "ACS Omega"

DOI: 10.1021/acsomega.5c00192

Abstract: Glutathione reductase (GR) is a homodimeric flavoenzyme that regenerates reduced glutathione, essential for cellular redox balance, with an active site cleft at the upper dimer interface. However, the role of intramolecular interactions within each monomer… read more here.

Keywords: pseudomonas mandelii; hydrophobic interactions; dimer interface; glutathione reductase ... See more keywords

Functional and Structural Roles of the Dimer Interface in the Activity and Stability of Clostridium butyricum 1,3-Propanediol Oxidoreductase.

Sign Up to like & get
recommendations!
Published in 2022 at "ACS synthetic biology"

DOI: 10.1021/acssynbio.1c00555

Abstract: Biosynthesis of 1,3-propanediol (1,3-PD) by 1,3-propanediol oxidoreductase (PDOR) is often limited by the stability issues. To address this issue, the goal of the present study was to engineer the Clostridium butyricum PDOR dimeric interface. The… read more here.

Keywords: propanediol; dimer interface; activity; stability ... See more keywords

Filamin C dimerisation is regulated by HSPB7

Sign Up to like & get
recommendations!
Published in 2025 at "Nature Communications"

DOI: 10.1038/s41467-025-58889-x

Abstract: The biomechanical properties and responses of tissues underpin a variety important of physiological functions and pathologies. In striated muscle, the actin-binding protein filamin C (FLNC) is a key protein whose variants causative for a wide… read more here.

Keywords: filamin dimerisation; dimerisation regulated; dimer interface; hetero dimer ... See more keywords

Molecular Interplay between the Dimer Interface and the Substrate-Binding Site of Human Peptidylarginine Deiminase 4

Sign Up to like & get
recommendations!
Published in 2017 at "Scientific Reports"

DOI: 10.1038/srep42662

Abstract: Our previous studies suggest that the fully active form of Peptidylarginine deiminase 4 (PAD4) should be a dimer and not a monomer. This paper provides a plausible mechanism for the control of PAD4 catalysis by… read more here.

Keywords: substrate binding; dimer interface; loop;

Chloroplast Preproteins Bind to the Dimer Interface of the Toc159 Receptor during Import1[OPEN]

Sign Up to like & get
recommendations!
Published in 2017 at "Plant Physiology"

DOI: 10.1104/pp.16.01952

Abstract: Preprotein-binding sites are mapped to the dimer interface and the switch II region of the Toc159 GTPase domain. Most chloroplast proteins are synthesized in the cytosol as higher molecular weight preproteins and imported via the… read more here.

Keywords: chloroplast; gtpase domain; dimer interface; receptor ... See more keywords
Photo from wikipedia

How Single Amino Acid Substitutions Can Disrupt a Protein Hetero-Dimer Interface: Computational and Experimental Studies of the LigAB Dioxygenase from Sphingobium sp. Strain SYK-6

Sign Up to like & get
recommendations!
Published in 2023 at "International Journal of Molecular Sciences"

DOI: 10.3390/ijms24076319

Abstract: Protocatechuate 4,5-dioxygenase (LigAB) is a heterodimeric enzyme that catalyzes the dioxygenation of multiple lignin derived aromatic compounds. The active site of LigAB is at the heterodimeric interface, with specificity conferred by the alpha subunit and… read more here.

Keywords: dimer interface; single amino; interface; catalytically active ... See more keywords