scholarly journals Role of Water in Ligand Binding to Maltose-Binding Protein: Insight from a New Docking Protocol Based on the 3D-RISM-KH Molecular Theory of Solvation

2015 ◽  
Vol 55 (2) ◽  
pp. 317-328 ◽  
Author(s):  
WenJuan Huang ◽  
Nikolay Blinov ◽  
David S. Wishart ◽  
Andriy Kovalenko
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Molecular Theory ◽  
Docking Protocol

Tritium NMR spectroscopy of ligand binding to maltose-binding protein

Biochemistry ◽  
1991 ◽  
Vol 30 (22) ◽  
pp. 5524-5531 ◽  
Author(s):  
Kalle Gehring ◽  
Philip G. Williams ◽  
Jeffrey G. Pelton ◽  
Hiromi Morimoto ◽  
David E. Wemmer
Keyword(s):  
Nmr Spectroscopy ◽  
Ligand Binding ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Tritium Nmr

scholarly journals Exploring the Role of Integral Membrane Proteins in ATP-Binding Cassette Transporters: Analysis of a Collection of MalG Insertion Mutants

1998 ◽  
Vol 180 (9) ◽  
pp. 2507-2514 ◽  
Author(s):  
Bryn D. Nelson ◽  
Beth Traxler
Keyword(s):  
Membrane Proteins ◽  
Cytoplasmic Membrane ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Integral Membrane Proteins ◽  
Atp Binding ◽  
Mutant Proteins ◽  
Transport Complex ◽  
Atp Binding Cassette

ABSTRACT The maltose transport complex of Escherichia coli is a well-studied example of an ATP-binding cassette transporter. The complex, containing one copy each of the integral membrane proteins MalG and MalF and two copies of the peripheral cytoplasmic membrane protein MalK, interacts with the periplasmic maltose-binding protein to efficiently translocate maltose and maltodextrins across the bacterial cytoplasmic membrane. To investigate the role of MalG both in MalFGK2 assembly interactions and in subsequent transport interactions, we isolated and characterized 18 different MalG mutants, each containing a 31-residue insertion in the protein. Eight insertions mapping to distinct hydrophilic regions of MalG permitted either assembly or both assembly and transport interactions to occur. In particular, we isolated two insertions mapping to extracytoplasmic (periplasmic) regions of MalG which preserved both assembly and transport abilities, suggesting that these are permissive sites in the protein. Another periplasmic insertion seems to affect only transport-specific interactions between MalG and maltose-binding protein, defining a novel class of MalG mutants. Finally, four MalG mutant proteins, although stably expressed, are unable to assemble into the MalFGK2 complex. These mutants contain insertions in only two different hydrophilic regions of MalG, consistent with the notion that a restricted number of domains in this protein are critical complex assembly determinants. These MalG mutants will allow us to further explore the intermolecular interactions of this model transporter.

The interrelationship between ligand binding and self-association of the folate binding protein. The role of detergent–tryptophan interaction

2011 ◽  
Vol 1810 (12) ◽  
pp. 1330-1339 ◽  
Author(s):  
Jan Holm ◽  
Christian Schou ◽  
Linnea N. Babol ◽  
Anders J. Lawaetz ◽  
Susanne W. Bruun ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Folate Binding Protein ◽  
Self Association

scholarly journals Mechanical Strength and Inhibition of theStaphylococcus aureusCollagen-Binding Protein Cna

mBio ◽  
2016 ◽  
Vol 7 (5) ◽  
Author(s):  
Philippe Herman-Bausier ◽  
Claire Valotteau ◽  
Giampiero Pietrocola ◽  
Simonetta Rindi ◽  
David Alsteens ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Monoclonal Antibodies ◽  
Ligand Binding ◽  
Mechanical Strength ◽  
Mechanical Response ◽  
Binding Protein ◽  
Adhesion Proteins ◽  
High Affinity ◽  
Living Bacteria

ABSTRACTThe bacterial pathogenStaphylococcus aureusexpresses a variety of cell surface adhesion proteins that bind to host extracellular matrix proteins. Among these, the collagen (Cn)-binding protein Cna plays important roles in bacterium-host adherence and in immune evasion. While it is well established that the A region of Cna mediates ligand binding, whether the repetitive B region has a dedicated function is not known. Here, we report the direct measurement of the mechanical strength of Cna-Cn bonds on living bacteria, and we quantify the antiadhesion activity of monoclonal antibodies (MAbs) targeting this interaction. We demonstrate that the strength of Cna-Cn bondsin vivois very strong (~1.2 nN), consistent with the high-affinity “collagen hug” mechanism. The B region is required for strong ligand binding and has been found to function as a spring capable of sustaining high forces. This previously undescribed mechanical response of the B region is of biological significance as it provides a means to project the A region away from the bacterial surface and to maintain bacterial adhesion under conditions of high forces. We further quantified the antiadhesion activity of MAbs raised against the A region of Cna directly on living bacteria without the need for labeling or purification. Some MAbs are more efficient in blocking single-cell adhesion, suggesting that they act as competitive inhibitors that bind Cna residues directly involved in ligand binding. This report highlights the role of protein mechanics in activating the function of staphylococcal adhesion proteins and emphasizes the potential of antibodies to prevent staphylococcal adhesion and biofilm formation.IMPORTANCECna is a collagen (Cn)-binding protein fromStaphylococcus aureusthat is involved in pathogenesis. Currently, we know little about the functional role of the repetitive B region of the protein. Here, we unravel the mechanical strength of Cna in living bacteria. We show that single Cna-Cn bonds are very strong, reflecting high-affinity binding by the collagen hug mechanism. We discovered that the B region behaves as a nanospring capable of sustaining high forces. This unanticipated mechanical response, not previously described for any staphylococcal adhesin, favors a model in which the B region has a mechanical function that is essential for strong ligand binding. Finally, we assess the antiadhesion activity of monoclonal antibodies against Cna, suggesting that they could be used to inhibitS. aureusadhesion.

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