Results 41 to 50 of about 142,532 (273)

The structure of bacterial outer membrane proteins

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2002
Integral membrane proteins come in two types, alpha-helical and beta-barrel proteins. In both types, all hydrogen bonding donors and acceptors of the polypeptide backbone are completely compensated and buried while nonpolar side chains point to the membrane. The alpha-helical type is more abundant and occurs in cytoplasmic (or inner) membranes, whereas
openaire   +3 more sources

Assembly of β-barrel proteins into bacterial outer membranes

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014
Membrane proteins with a β-barrel topology are found in the outer membranes of Gram-negative bacteria and in the plastids and mitochondria of eukaryotic cells. The assembly of these membrane proteins depends on a protein folding reaction (to create the barrel) and an insertion reaction (to integrate the barrel within the outer membrane).
Selkrig, Joel, Leyton, Denisse, Webb, Chaille T, Lithgow, Trevor   +3 more
openaire   +3 more sources

Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation

mBio, 2021
Outer membrane proteins (OMPs) play critical roles in bacterial pathogenicity and provide a new niche for antibiotic development. A comprehensive understanding of the OMP quality control network will strongly impact antimicrobial discovery.
Wei He, Gangjin Yu, Tianpeng Li, Ling Bai, Yuanyuan Yang, Zixiao Xue, Yonghao Pang, Dana Reichmann, Sebastian Hiller, Lichun He, Maili Liu, Shu Quan   +11 more
doaj   +1 more source

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

FEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang, Grace Du, Charity Yongo‐Luwawa, Angelina Lu, Brett Kinrade, Kim Munro, Karl E. Klose, William D. Lubell, Peter Davies, Shuaiqi Guo   +9 more
wiley   +1 more source

Polymyxins slow down lateral diffusion of proteins and lipopolysaccharide in the E. coli outer membrane

Communications Biology
Polymyxins are often administered as last resort antibiotics for Gram-negative bacterial infections. However, given unwanted side-effects, efficacy and recent reports of resistance against polymyxins, there is an urgency to develop alternatives.
Dheeraj Prakaash, Syma Khalid
doaj   +1 more source

Analyzing the molecular mechanism of lipoprotein localization in Brucella

Frontiers in Microbiology, 2015
Bacterial lipoproteins possess comprehensive structure and functionality, ranging from bacterial physiology to pathogenic processes. As such many lipoproteins, originating from Brucella are exploited as potential vaccines to countermeasure brucellosis ...
Shivani eGoolab, Shivani eGoolab, Robyn Lindsay Roth, Henriette evan Heerden, Michael Craig Crampton   +4 more
doaj   +1 more source

Substrate specificity of Burkholderia pseudomallei multidrug transporters is influenced by the hydrophilic patch in the substrate‐binding pocket

FEBS Letters, EarlyView.
Multidrug transporters BpeB and BpeF from the Gram‐negative pathogen Burkholderia pseudomallei have a hydrophilic patch in their substrate‐binding pocket. Drug susceptibility tests and growth curve analyses using an Escherichia coli recombinant expression system revealed that the hydrophilic patches of BpeB and BpeF are involved in the substrate ...
Ui Okada, Satoshi Murakami
wiley   +1 more source

Mechanisms of parasite‐mediated disruption of brain vessels

FEBS Letters, EarlyView.
Parasites can affect the blood vessels of the brain, often causing serious neurological problems. This review explains how different parasites interact with and disrupt these vessels, what this means for brain health, and why these processes matter. Understanding these mechanisms may help us develop better ways to prevent or treat brain infections in ...
Leonor Loira, Sílvia Arroz‐Madeira, Cláudio A. Franco, Sara Silva Pereira   +3 more
wiley   +1 more source

Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM

Nature Communications, 2021
The β-barrel assembly machinery (BAM) assists the folding and membrane insertion of bacterial outer membrane proteins. Here, the authors report structural characterization of BAM in lipid environment and in complex with the client protein EspP integrated
Runrun Wu, Jeremy W. Bakelar, Karl Lundquist, Zijian Zhang, Katie M. Kuo, David Ryoo, Yui Tik Pang, Chen Sun, Tommi White, Thomas Klose, Wen Jiang, James C. Gumbart, Nicholas Noinaj   +12 more
doaj   +1 more source

In situ molecular organization and heterogeneity of the Legionella Dot/Icm T4SS

FEBS Letters, EarlyView.
We present a nearly complete in situ model of the Legionella Dot/Icm type IV secretion system, revealing its central secretion channel and identifying new components. Using cryo‐electron tomography with AI‐based modeling, our work highlights the structure, variability, and mechanism of this complex nanomachine, advancing understanding of bacterial ...
Przemysław Dutka, Yuxi Liu, Stefano Maggi, Debnath Ghosal, Jue Wang, Prashant P. Damke, Stephen D. Carter, Wei Zhao, Sukhithasri Vijayrajratnam, Joseph P. Vogel, Carrie L. Shaffer, Grant J. Jensen   +11 more
wiley   +1 more source