Binding mechanisms in supramolecular complexes
HJ Schneider - Angewandte Chemie International Edition, 2009 - Wiley Online Library
Forces to reckon with: Supramolecular complexes, such as the one shown, are normally
based on a combination of different interactions such as ion pairing, hydrogen bonds, and …
based on a combination of different interactions such as ion pairing, hydrogen bonds, and …
How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria
J Deutscher, C Francke, PW Postma - Microbiology and molecular …, 2006 - Am Soc Microbiol
The phosphoenolpyruvate (PEP): carbohydrate phosphotransferase system (PTS) is found
only in bacteria, where it catalyzes the transport and phosphorylation of numerous …
only in bacteria, where it catalyzes the transport and phosphorylation of numerous …
Carbohydrate–aromatic interactions
JL Asensio, A Ardá, FJ Cañada… - Accounts of chemical …, 2013 - ACS Publications
The recognition of saccharides by proteins has far reaching implications in biology,
technology, and drug design. Within the past two decades, researchers have directed …
technology, and drug design. Within the past two decades, researchers have directed …
Structure and Mechanism of the Lactose Permease of Escherichia coli
J Abramson, I Smirnova, V Kasho, G Verner… - Science, 2003 - science.org
Membrane transport proteins that transduce free energy stored in electrochemical ion
gradients into a concentration gradient are a major class of membrane proteins. We report …
gradients into a concentration gradient are a major class of membrane proteins. We report …
Lessons from lactose permease
L Guan, HR Kaback - Annu. Rev. Biophys. Biomol. Struct., 2006 - annualreviews.org
An X-ray structure of the lactose permease of Escherichia coli (LacY) in an inward-facing
conformation has been solved. LacY contains N-and C-terminal domains, each with six …
conformation has been solved. LacY contains N-and C-terminal domains, each with six …
The alternating-access mechanism of MFS transporters arises from inverted-topology repeats
S Radestock, LR Forrest - Journal of molecular biology, 2011 - Elsevier
Lactose permease (LacY) is the prototype of the major facilitator superfamily (MFS) of
secondary transporters. Available structures of LacY reveal a state in which the substrate is …
secondary transporters. Available structures of LacY reveal a state in which the substrate is …
[HTML][HTML] Structure-based mechanism for Na+/melibiose symport by MelB
AS Ethayathulla, MS Yousef, A Amin, G Leblanc… - Nature …, 2014 - nature.com
The bacterial melibiose permease (MelB) belongs to the glycoside–pentoside–hexuronide:
cation symporter family, a part of the major facilitator superfamily (MFS). Structural …
cation symporter family, a part of the major facilitator superfamily (MFS). Structural …
Structural determination of wild-type lactose permease
Here we describe an x-ray structure of wild-type lactose permease (LacY) from Escherichia
coli determined by manipulating phospholipid content during crystallization. The structure …
coli determined by manipulating phospholipid content during crystallization. The structure …
The whole is bigger than the sum of its parts: drug transport in the context of two membranes with active efflux
VV Rybenkov, HI Zgurskaya, C Ganguly… - Chemical …, 2021 - ACS Publications
Cell envelope plays a dual role in the life of bacteria by simultaneously protecting it from a
hostile environment and facilitating access to beneficial molecules. At the heart of this ability …
hostile environment and facilitating access to beneficial molecules. At the heart of this ability …
Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY
Cation‐coupled active transport is an essential cellular process found ubiquitously in all
living organisms. Here, we present two novel ligand‐free X‐ray structures of the lactose …
living organisms. Here, we present two novel ligand‐free X‐ray structures of the lactose …