[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 …

[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 …

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 …

Crystal structure of the carnitine transporter and insights into the antiport mechanism

L Tang, L Bai, W Wang, T Jiang - Nature structural & molecular biology, 2010 - nature.com
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 …

[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 …

[HTML][HTML] Oligomeric structure of the carnitine transporter CaiT from Escherichia coli

KR Vinothkumar, S Raunser, H Jung… - Journal of Biological …, 2006 - ASBMB
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 …

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 …

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 …

Investigations of dimethylglycine, glycine betaine, and ectoine uptake by a betaine-carnitine-choline transporter family transporter with diverse substrate specificity in …

GJ Gregory, A Dutta, V Parashar… - Journal of Bacteriology, 2020 - Am Soc Microbiol
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 …

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 …