Dynamics of the E. coli β-Clamp Dimer Interface and Its Influence on DNA Loading.
Sign Up to like & getrecommendations! 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 & getrecommendations! 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
Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems.
Sign Up to like & getrecommendations! 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 & getrecommendations! 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
Functional and Structural Roles of the Dimer Interface in the Activity and Stability of Clostridium butyricum 1,3-Propanediol Oxidoreductase.
Sign Up to like & getrecommendations! 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
Molecular Interplay between the Dimer Interface and the Substrate-Binding Site of Human Peptidylarginine Deiminase 4
Sign Up to like & getrecommendations! 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 & getrecommendations! 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
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 & getrecommendations! 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
Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors
Sign Up to like & getrecommendations! Published in 2021 at "Membranes"
DOI: 10.3390/membranes11080613
Abstract: Kainate receptors are members of the ionotropic glutamate receptor family. They form cation-specific transmembrane channels upon binding glutamate that desensitize in the continued presence of agonists. Concanavalin A (Con-A), a lectin, stabilizes the active open-channel… read more here.
Keywords: dimer interface; kainate receptor; gluk2; receptor ... See more keywords