An aspartate-specific solute-binding protein regulates protein kinase G activity to control glutamate metabolism in mycobacteria
N Bhattacharyya, IN Nkumama, Z Newland-Smith… - MBio, 2018 - Am Soc Microbiol
Signaling by serine/threonine phosphorylation controls diverse processes in bacteria, and
identification of the stimuli that activate protein kinases is an outstanding question in the …
identification of the stimuli that activate protein kinases is an outstanding question in the …
Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo …
Arginine-binding protein from the extremophile Thermotoga maritima is a 27.7 kDa protein
possessing the typical two-domain structure of the periplasmic binding proteins family. The …
possessing the typical two-domain structure of the periplasmic binding proteins family. The …
A Loose Domain Swapping Organization Confers a Remarkable Stability to the Dimeric Structure of the Arginine Binding Protein from Thermotoga maritima
The arginine binding protein from Thermatoga maritima (TmArgBP), a substrate binding
protein (SBP) involved in the ABC system of solute transport, presents a number of …
protein (SBP) involved in the ABC system of solute transport, presents a number of …
[HTML][HTML] Amino acid transport in thermophiles: characterization of an arginine-binding protein from Thermotoga maritima. 3. Conformational dynamics and stability
Arginine-binding protein from Thermotoga maritima (TmArgBP) is a 27.7 kDa protein
possessing the typical two domain structure of the periplasmic binding protein family. The …
possessing the typical two domain structure of the periplasmic binding protein family. The …
Engineering a switch-based biosensor for arginine using a Thermotoga maritima periplasmic binding protein
T Donaldson, L Iozzino, LJ Deacon, H Billones… - Analytical …, 2017 - Elsevier
The Thermotoga maritima arginine-binding protein (Tm ArgBP) has been modified to create
a reagentless fluorescent protein biosensor. Two design methods for biosensor construction …
a reagentless fluorescent protein biosensor. Two design methods for biosensor construction …
Guanidinium binding to proteins: The intriguing effects on the D1 and D2 domains of Thermotoga maritima Arginine Binding Protein and a comprehensive analysis of …
S Cozzolino, N Balasco, M Vigorita, A Ruggiero… - International Journal of …, 2020 - Elsevier
Abstract Thermotoga maritima Arginine Binding Protein has been extensively characterized
because of its peculiar features and its possible use as a biosensor. In this characterization …
because of its peculiar features and its possible use as a biosensor. In this characterization …
Domain swapping dissection in Thermotoga maritima arginine binding protein: How structural flexibility may compensate destabilization
Abstract Thermotoga maritima Arginine Binding Protein (TmArgBP) is a valuable candidate
for arginine biosensing in diagnostics. This protein is endowed with unusual structural …
for arginine biosensing in diagnostics. This protein is endowed with unusual structural …
The characterization of Thermotoga maritima Arginine Binding Protein variants demonstrates that minimal local strains have an important impact on protein stability
N Balasco, G Smaldone, M Vigorita, P Del Vecchio… - Scientific Reports, 2019 - nature.com
The Ramachandran plot is a versatile and valuable tool that provides fundamental
information for protein structure determination, prediction, and validation. The structural …
information for protein structure determination, prediction, and validation. The structural …
Proline 235 plays a key role in the regulation of the oligomeric states of Thermotoga maritima Arginine Binding Protein
G Smaldone, M Vigorita, A Ruggiero, N Balasco… - … et Biophysica Acta (BBA …, 2016 - Elsevier
Abstract The Arginine Binding Protein isolated from Thermotoga maritima (TmArgBP) is a
protein endowed with several peculiar properties. We have previously shown that TmArgBP …
protein endowed with several peculiar properties. We have previously shown that TmArgBP …
Tryptophan-scanning mutagenesis of the ligand binding pocket in Thermotoga maritima arginine-binding protein
LJ Deacon, H Billones, AA Galyean, T Donaldson… - Biochimie, 2014 - Elsevier
The Thermotoga maritima arginine binding protein (TmArgBP) is a member of the
periplasmic binding protein superfamily. As a highly thermostable protein, TmArgBP has …
periplasmic binding protein superfamily. As a highly thermostable protein, TmArgBP has …