scholarly journals Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein

1998 ◽  
Vol 7 (10) ◽  
pp. 2136-2142 ◽  
Author(s):  
Sébastien Raffy ◽  
Nathalie Sassoon ◽  
Maurice Hofnung ◽  
Jean-Michel Betton
Keyword(s):  
Tertiary Structure ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Structure Dependence

Correlation of competence for export with lack of tertiary structure of the mature species: A study in vivo of maltose-binding protein in E. coli

Cell ◽  
1986 ◽  
Vol 46 (6) ◽  
pp. 921-928 ◽  
Author(s):  
Linda L. Randall ◽  
Simon J.S. Hardy
Keyword(s):  
Tertiary Structure ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
E Coli

scholarly journals The Molten Globule State of Maltose-Binding Protein: Structural and Thermodynamic Characterization by EPR Spectroscopy and Isothermal Titration Calorimetry

2020 ◽  
Vol 51 (9-10) ◽  
pp. 877-886
Author(s):  
Chen Nickolaus ◽  
Carolyn Vargas ◽  
Jörg Reichenwallner ◽  
Mohammed Chakour ◽  
Benjamin Selmke ◽  
...  
Keyword(s):  
Epr Spectroscopy ◽  
Tertiary Structure ◽  
Binding Protein ◽  
Molten Globule ◽  
Spin Labeling ◽  
Maltose Binding Protein ◽  
Titration Calorimetry ◽  
Native State ◽  
Paramagnetic Resonance ◽  
Distance Information

Abstract Employing site-directed spin labeling (SDSL), the structure of maltose-binding protein (MBP) had previously been studied in the native state by electron paramagnetic resonance (EPR) spectroscopy. Several spin-labeled double cysteine mutants were distributed all over the structure of this cysteine-free protein and revealed distance information between the nitroxide residues from double electron–electron resonance (DEER). The results were in good agreement with the known X-ray structure. We have now extended these studies to the molten globule (MG) state, a folding intermediate, which can be stabilized around pH 3 and that is characterized by secondary but hardly any tertiary structure. Instead of clearly defined distance features as found in the native state, several additional characteristics indicate that the MG structure of MBP contains different polypeptide chain and domain orientations. MBP is also known to bind its substrate maltose even in MG state although with lower affinity. Additionally, we have now created new mutants allowing for spin labeling at or near the active site. Our data confirm an already preformed ligand site structure in the MG explaining its substrate binding capability and thus most probably serving as a nucleation center for the final native structure.

Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding

2001 ◽  
Vol 306 (5) ◽  
pp. 1115-1126 ◽  
Author(s):  
Xiaoqun Duan ◽  
Jason A Hall ◽  
Hiroshi Nikaido ◽  
Florante A Quiocho
Keyword(s):  
Ligand Binding ◽  
Crystal Structures ◽  
Tertiary Structure ◽  
Binding Protein ◽  
Maltose Binding Protein

scholarly journals Intragenic reversion mutations that improve export of maltose-binding protein in Escherichia coli malE signal sequence mutants.

1986 ◽  
Vol 261 (7) ◽  
pp. 3389-3395
Author(s):  
J P Ryan ◽  
M C Duncan ◽  
V A Bankaitis ◽  
P J Bassford
Keyword(s):  
Escherichia Coli ◽  
Signal Sequence ◽  
Binding Protein ◽  
Maltose Binding Protein

Production of MBP(maltose binding protein)-GroES fusion protein and utilization to stimulate GroEL-mediated protein refolding

1998 ◽  
Vol 85 (1) ◽  
pp. 69-73 ◽  
Author(s):  
Yoshiyuki Ishii ◽  
Kaoru Murakami ◽  
Hiroaki I.-Ogawa ◽  
Akihiko Kondo ◽  
Yasuhiko Kato
Keyword(s):  
Fusion Protein ◽  
Binding Protein ◽  
Protein Refolding ◽  
Maltose Binding Protein

scholarly journals Maltose chemotaxis involves residues in the N-terminal and C-terminal domains on the same face of maltose-binding protein

1992 ◽  
Vol 267 (32) ◽  
pp. 22813-22820
Author(s):  
Y Zhang ◽  
C Conway ◽  
M Rosato ◽  
Y Suh ◽  
M.D. Manson
Keyword(s):  
Binding Protein ◽  
Maltose Binding Protein ◽  
Terminal Domains
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