A reciprocating twin-channel model for ABC transporters

PM Jones, AM George - Quarterly reviews of biophysics, 2014 - cambridge.org
ABC transporters comprise a large, diverse, and ubiquitous superfamily of membrane active
transporters. Their core architecture is a dimer of dimers, comprising two transmembrane …

The substrate-binding domains of the osmoregulatory ABC importer OpuA transiently interact

M van den Noort, P Drougkas, C Paulino, B Poolman - Elife, 2024 - elifesciences.org
Bacteria utilize various strategies to prevent internal dehydration during hypertonic stress. A
common approach to countering the effects of the stress is to import compatible solutes such …

Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo …

A Ausili, M Staiano, J Dattelbaum, A Varriale, A Capo… - Life, 2013 - mdpi.com
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 …

A Loose Domain Swapping Organization Confers a Remarkable Stability to the Dimeric Structure of the Arginine Binding Protein from Thermotoga maritima

A Ruggiero, JD Dattelbaum, M Staiano, R Berisio… - PLoS …, 2014 - journals.plos.org
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 …

Destabilization of the D2 domain of Thermotoga maritima arginine binding protein induced by guanidinium thiocyanate and its counteraction by stabilizing agents

G Izzi, A Paladino, R Oliva, G Barra, A Ruggiero… - Protein …, 2024 - Wiley Online Library
D2 is a structural and cooperative domain of Thermotoga maritima Arginine Binding Protein,
that possesses a remarkable conformational stability, with a denaturation temperature of …

Substrate recognition and transport behavior analyses of amino acid antiporter with coarse-grained models

S Chang, J Hu, P Lin, X Jiao, X Tian - Molecular BioSystems, 2010 - pubs.rsc.org
The L-arginine (Arg)/agmatine (Agm) antiporter AdiC is a vital transport protein of the
arginine-dependent extreme acid resistance system of enteric bacteria. Recently, both …

Periplasmic binding protein dimer has a second allosteric event tied to ligand binding

L Li, S Ghimire-Rijal, SL Lucas, CB Stanley… - Biochemistry, 2017 - ACS Publications
The ligand-induced conformational changes of periplasmic binding proteins (PBP) play a
key role in the acquisition of metabolites in ATP binding cassette (ABC) transport systems …

[HTML][HTML] Amino acid transport in thermophiles: characterization of an arginine-binding protein from Thermotoga maritima. 3. Conformational dynamics and stability

A Ausili, A Pennacchio, M Staiano… - … of Photochemistry and …, 2013 - Elsevier
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 …

Characterization of Cationic Amino Acid Binding Protein from Candidatus Liberibacter Asiaticus and in Silico Study to Identify Potential Inhibitor Molecules

S Lonare, DN Gupta, H Kaur, S Rode, S Verma… - The Protein …, 2024 - Springer
Cationic amino acid binding protein (CLasArgBP), one of the two amino acid binding
receptor in Candidatus Liberibacter asiaticus (CLas), is predominately expressed in citrus …

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 …