Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling
Cell 162(6):1431 (2015)
SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins.
Science 348(6241):1361 (2015)
G protein-coupled receptors (GPCRs) relay diverse extracellular signals into cells by catalyzing nucleotide release from heterotrimeric G proteins, but the mechanism underlying this quintessential molecular signaling event has remained unclear. Here we use atomic-level simulations to elucidate t...
Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling.
Cell 161(5):1101 (2015)
G-protein-coupled receptors (GPCRs) transduce signals from the extracellular environment to intracellular proteins. To gain structural insight into the regulation of receptor cytoplasmic conformations by extracellular ligands during signaling, we examine the structural dynamics of the cytoplasmi...
Extracellular loop 4 of the proline transporter PutP controls the periplasmic entrance to ligand binding sites.
Structure 22(5):769 (2014)
The Na(+)/proline symporter (PutP), like several other Na(+)-coupled symporters, belongs to the so-called LeuT-fold structural family, which features ten core transmembrane domains (cTMs) connected by extra- and intracellular loops. The role of these loops has been discussed in context with the ...
Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide.
Nature 497(7447):137 (2013)
The functions of G-protein-coupled receptors (GPCRs) are primarily mediated and modulated by three families of proteins: the heterotrimeric G proteins, the G-protein-coupled receptor kinases (GRKs) and the arrestins. G proteins mediate activation of second-messenger-generating enzymes and other ...
The sodium/proline transporter PutP of Helicobacter pylori.
PLoS ONE 8(12):e83576 (2013)
Helicobacter pylori is cause of chronic gastritis, duodenal ulcer and gastric carcinoma in humans. L-proline is a preferred energy source of the microaerophilic bacterium. Previous analyses revealed that HpputP and HpputA, the genes that are predicted to play a central role in proline metabolism...
Initial steps of photosystem II de novo assembly and preloading with manganese take place in biogenesis centers in Synechocystis.
Plant Cell 24(2):660 (2012)
In the cyanobacterium Synechocystis sp PCC 6803, early steps in thylakoid membrane (TM) biogenesis are considered to take place in specialized membrane fractions resembling an interface between the plasma membrane (PM) and TM. This region (the PratA-defined membrane) is defined by the presence o...
The Na⁺/L-proline transporter PutP.
Frontiers in Bioscience 17:745 (2012)
The Na⁺/L-proline transporter PutP is a member of the Na⁺/solute symporter family (TC 2A.21, SLC5), which contains several hundred proteins of pro- and eukaryotic origin. Within the family, the capability of L-proline uptake is restricted to proteins of prokaryotes. PutP contributes to the use o...
Homology model of the Na+/proline transporter PutP of Escherichia coli and its functional implications.
Journal of Molecular Biology 406(1):59 (2011)
Na(+)/solute symporters are essential membrane integrated proteins that couple the flow of Na(+) ions driven by electrochemical Na(+) gradients to the transport of solutes across biological membranes. Here, we used a combination of molecular modeling techniques and evolutionary conservation anal...
Backbone Structure of Transmembrane Domain IX of the Na+/Proline Transporter PutP ofEscherichia coli
Biophysical Journal 96(1):217 (2009)
The backbone structure is determined by site-directed spin labeling, double electron electron resonance measurements of distances, and modeling in terms of a helix-loop-helix construct for a transmembrane domain that is supposed to line the translocation pathway in the 54.3 kDa Na
Function of transmembrane domain IX in the Na+/proline transporter PutP.
Journal of Molecular Biology 382(4):884 (2008)
Selected residues of transmembrane domain (TM) IX were previously shown to play key roles in ligand binding and transport in members of the Na(+)/solute symporter family. Using the Na(+)/proline transporter PutP as a model, a complete Cys scanning mutagenesis of TM IX (positions 324 to 351) was ...
Role of Ser-340 and Thr-341 in transmembrane domain IX of the Na+/proline transporter PutP of Escherichia coli in ligand binding and transport.
Journal of Biological Chemistry 283(8):4921 (2008)
The Na+/solute symporter family comprises more than 400 members of pro- and eukaryotic origin. Using the Na+/proline transporter PutP of Escherichia coli as a model, the role of two conserved residues, Ser-340 and Thr-341, is investigated to obtain insights into the mechanism of transport cataly...
Assessing oligomerization of membrane proteins by four-pulse DEER: pH-dependent dimerization of NhaA Na+/H+ antiporter of E. coli.
Biophysical Journal 89(2):1328 (2005)
The pH dependence of the structure of the main Na(+)/H(+) antiporter NhaA of Escherichia coli is studied by continuous-wave (CW) and pulse electron paramagnetic resonance (EPR) techniques on singly spin-labeled mutants. Residues 225 and 254 were selected for site-directed spin labeling, as previ...
Assessing Oligomerization of Membrane Proteins by Four-Pulse DEER: pH-Dependent Dimerization of NhaA Na+/H+Antiporter ofE. coli
Biophysical Journal 89(2):1328 (2005)
The pH dependence of the structure of the main Na
+ antiporter NhaA of
Escherichia coli is studied by continuous-wave (CW) and pulse electron paramagnetic resonance (EPR) techniques on singly spin-labeled mutants. Residues 225 and 254 were selected for site-directed s...