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 …

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 …

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 …

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 …

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 …

High-speed atomic force microscopy reveals a three-state elevator mechanism in the citrate transporter CitS

S Maity, G Trinco, P Buzón… - Proceedings of the …, 2022 - National Acad Sciences
The secondary active transporter CitS shuttles citrate across the cytoplasmic membrane of
gram-negative bacteria by coupling substrate translocation to the transport of two Na+ ions …

[HTML][HTML] Substrate discrimination by ergothioneine transporter SLC22A4 and carnitine transporter SLC22A5: gain-of-function by interchange of selected amino acids

P Bacher, S Giersiefer, M Bach, C Fork… - … et Biophysica Acta (BBA …, 2009 - Elsevier
ETT (originally designated as OCTN1; human gene symbol SLC22A4) and CTT (OCTN2;
SLC22A5) are highly specific transporters of ergothioneine and carnitine, respectively …

Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism

P Stenmark, D Gurmu, P Nordlund - Biochemistry, 2004 - ACS Publications
Carnitine is an important molecule in human metabolism, mainly because of its role in the
transport of long-chain fatty acids across the inner mitochondrial membrane. Escherichia coli …

The mitochondrial carnitine acyl-carnitine carrier (SLC25A20): molecular mechanisms of transport, role in redox sensing and interaction with drugs

A Tonazzi, N Giangregorio, L Console, F Palmieri… - Biomolecules, 2021 - mdpi.com
The SLC25A20 transporter, also known as carnitine acyl-carnitine carrier (CAC), catalyzes
the transport of short, medium and long carbon chain acyl-carnitines across the …

Functional characterization of residues within the carnitine/acylcarnitine translocase RX2PANAAXF distinct motif

J Ramon De Lucas, J Ramon De Lucas… - Molecular Membrane …, 2008 - Taylor & Francis
The mitochondrial carnitine/acylcarnitine carrier (CAC) is characterized by the presence of a
distinct motif, RXXPANAAXF, within its sixth transmembrane α-helix. In this study, we …