[HTML][HTML] Comparison of the functional properties of trimeric and monomeric CaiT of Escherichia coli
S Bracher, D Hilger, K Guérin, Y Polyhach, G Jeschke… - Scientific reports, 2019 - nature.com
Secondary transporters exist as monomers, dimers or higher state oligomers. The
significance of the oligomeric state is only partially understood. Here, the significance of the …
significance of the oligomeric state is only partially understood. Here, the significance of the …
[HTML][HTML] CaiT of Escherichia coli, a new transporter catalyzing L-carnitine/γ-butyrobetaine exchange
H Jung, M Buchholz, J Clausen, M Nietschke… - Journal of Biological …, 2002 - ASBMB
l-Carnitine is essential for β-oxidation of fatty acids in mitochondria. Bacterial metabolic
pathways are used for the production of this medically important compound. Here, we report …
pathways are used for the production of this medically important compound. Here, we report …
Arginine oscillation explains Na+ independence in the substrate/product antiporter CaiT
S Kalayil, S Schulze… - Proceedings of the …, 2013 - National Acad Sciences
Most secondary-active transporters transport their substrates using an electrochemical ion
gradient. In contrast, the carnitine transporter (CaiT) is an ion-independent, l-carnitine/γ …
gradient. In contrast, the carnitine transporter (CaiT) is an ion-independent, l-carnitine/γ …
Crystal structure of the carnitine transporter and insights into the antiport mechanism
CaiT is a membrane antiporter that catalyzes the exchange of l-carnitine with γ-
butyrobetaine across the Escherichia coli membrane. To obtain structural insights into the …
butyrobetaine across the Escherichia coli membrane. To obtain structural insights into the …
[HTML][HTML] A conformational switch in a partially unwound helix selectively determines the pathway for substrate release from the carnitine/γ-butyrobetaine antiporter …
E Zomot, I Bahar - Journal of Biological Chemistry, 2012 - ASBMB
CaiT is a homotrimeric antiporter that exchanges l-carnitine (CRN) with γ-butyrobetaine
(GBB) across the bacterial membrane. Three structures have been resolved to date for CaiT …
(GBB) across the bacterial membrane. Three structures have been resolved to date for CaiT …
[HTML][HTML] Oligomeric structure of the carnitine transporter CaiT from Escherichia coli
The carnitine transporter CaiT from Escherichia coli belongs to the betaine, choline, and
carnitine transporter family of secondary transporters. It acts as an l-carnitine/γ-butyrobetaine …
carnitine transporter family of secondary transporters. It acts as an l-carnitine/γ-butyrobetaine …
Structural basis of Na+-independent and cooperative substrate/product antiport in CaiT
S Schulze, S Köster, U Geldmacher… - Nature, 2010 - nature.com
Transport of solutes across biological membranes is performed by specialized secondary
transport proteins in the lipid bilayer, and is essential for life. Here we report the structures of …
transport proteins in the lipid bilayer, and is essential for life. Here we report the structures of …
Structure, substrate selectivity determinants and membrane interactions of a Glutamate-specific TAXI TRAP binding protein from Vibrio cholerae.
JFS Davies, A Daab, N Massouh, C Kirkland… - bioRxiv, 2024 - biorxiv.org
Tripartite ATP independent periplasmic (TRAP) transporters are widespread in prokaryotes
and are responsible for the transport of a variety of different ligands, primarily organic acids …
and are responsible for the transport of a variety of different ligands, primarily organic acids …
Investigations of dimethylglycine, glycine betaine, and ectoine uptake by a betaine-carnitine-choline transporter family transporter with diverse substrate specificity in …
Fluctuations in osmolarity are one of the most prevalent stresses to which bacteria must
adapt, both hypo-and hyperosmotic conditions. Most bacteria cope with high osmolarity by …
adapt, both hypo-and hyperosmotic conditions. Most bacteria cope with high osmolarity by …
Bacterial over-expression of functionally active human CT2 (SLC22A16) carnitine transporter
M Galluccio, T Mazza, M Scalise, MC Sarubbi… - Molecular Biology …, 2022 - Springer
Background Escherichia coli is a widely used tool for the over-expression of human proteins
for studying structure and function. The toxicity of human proteins for E. coli often hampers …
for studying structure and function. The toxicity of human proteins for E. coli often hampers …