Structures and functions of mitochondrial ABC transporters

TA Schaedler, B Faust, CA Shintre… - Biochemical Society …, 2015 - portlandpress.com
A small number of physiologically important ATP-binding cassette (ABC) transporters are
found in mitochondria. Most are half transporters of the B group forming homodimers and …

Lysosomal targeting of the ABC transporter TAPL is determined by membrane-localized charged residues

P Graab, C Bock, K Weiss, A Hirth, N Koller… - Journal of Biological …, 2019 - ASBMB
The human lysosomal polypeptide ABC transporter TAPL (ABC subfamily B member 9,
ABCB9) transports 6–59-amino-acid-long polypeptides from the cytosol into lysosomes. The …

Crystallization and initial X-ray diffraction of BtuB, the integral membrane cobalamin transporter of Escherichia coli

DP Chimento, AK Mohanty, RJ Kadner… - … Section D: Biological …, 2003 - journals.iucr.org
BtuB, the cobalamin transporter from Escherichia coli, has been overexpressed, purified and
crystallized. The purified protein was solubilized in n-octyl tetraoxyethylene (C8E4) and was …

Structure of the human lipid exporter ABCB4 in a lipid environment

JA Olsen, A Alam, J Kowal, B Stieger… - Nature structural & …, 2020 - nature.com
ABCB4 is an ATP-binding cassette transporter that extrudes phosphatidylcholine into the
bile canaliculi of the liver. Its dysfunction or inhibition by drugs can cause severe, chronic …

An inventory of lysosomal ABC transporters

G Szakacs, R Abele - FEBS letters, 2020 - Wiley Online Library
ABC transporters fulfill diverse physiological functions in different cellular localizations
ranging from the plasma membrane to intracellular membranous compartments. Several …

Molecular structure and characterization of a novel murine ABC transporter, Abca13

SA Barros, RW Tennant, RE Cannon - Gene, 2003 - Elsevier
We report the isolation and structural characterization of the full-length gene and cDNA for a
novel mouse ATP-binding cassette (ABC) transporter, Abca13. The mRNA, isolated from …

Functional and structural characterization of an ECF-type ABC transporter for vitamin B12

JA Santos, S Rempel, STM Mous, CT Pereira… - Elife, 2018 - elifesciences.org
Vitamin B12 (cobalamin) is the most complex B-type vitamin and is synthetized exclusively
in a limited number of prokaryotes. Its biologically active variants contain rare organometallic …

Structural basis for mammalian vitamin B12 transport by transcobalamin

J Wuerges, G Garau, S Geremia… - Proceedings of the …, 2006 - National Acad Sciences
Cobalamin (Cbl, vitamin B12) serves for two essential cofactors in mammals. The pathway
for its intestinal absorption, plasma transport, and cellular uptake uses cell surface receptors …

A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization

N Tal, E Ovcharenko… - Proceedings of the …, 2013 - National Acad Sciences
In all kingdoms of life, ATP binding cassette (ABC) transporters are essential to many
cellular functions. In this large superfamily of proteins, two catalytic sites hydrolyze ATP to …

[HTML][HTML] Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking

BA Goetz, E Perozo, KP Locher - FEBS letters, 2009 - Elsevier
BtuCD is a type II ABC importer that catalyzes the translocation of vitamin B12 from the
periplasm into the cytoplasm of Escherichia coli. Crystal structures of BtuCD and the related …