TheE. ColiReplication Factor DnaC Protein Exists in Two Conformations with Different Nucleotide Binding Capabilities. I. Determination of the Binding Mechanism Using ATP and ADP Fluorescent Analogues†

Biochemistry ◽  
2002 ◽  
Vol 41 (28) ◽  
pp. 8907-8920 ◽  
Author(s):  
Roberto Galletto ◽  
Wlodzimierz Bujalowski
Keyword(s):  
Nucleotide Binding ◽  
Binding Mechanism ◽  
Dnac Protein ◽  
Fluorescent Analogues

The Nucleotide-Binding Site of the Escherichia coli DnaC Protein: Molecular Topography of DnaC Protein–Nucleotide Cofactor Complexes

2005 ◽  
Vol 43 (3) ◽  
pp. 331-354 ◽  
Author(s):  
Roberto Galletto ◽  
Maria J. Jezewska ◽  
Rodrigo Maillard ◽  
Wlodzimierz Bujalowski
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Dnac Protein

scholarly journals Co-crystallization of human inositol monophosphatase with the lithium mimetic L-690,330

2018 ◽  
Vol 74 (10) ◽  
pp. 973-978 ◽  
Author(s):  
Lucas Kraft ◽  
S. Mark Roe ◽  
Raj Gill ◽  
John R. Atack
Keyword(s):  
Bipolar Disorder ◽  
Side Effects ◽  
Gold Standard ◽  
Cell Signalling ◽  
Therapeutic Effects ◽  
Binding Mechanism ◽  
Manganese Ions ◽  
Inositol Monophosphatase ◽  
X Ray

Lithium, which is still the gold standard in the treatment of bipolar disorder, has been proposed to inhibit inositol monophosphatase (IMPase) and is hypothesized to exert its therapeutic effects by attenuating phosphatidylinositol (PI) cell signalling. Drug-discovery efforts have focused on small-molecule lithium mimetics that would specifically inhibit IMPase without exhibiting the undesired side effects of lithium. L-690,330 is a potent bisphosphonate substrate-based inhibitor developed by Merck Sharp & Dohme. To aid future structure-based inhibitor design, determination of the exact binding mechanism of L-690,330 to IMPase was of interest. Here, the high-resolution X-ray structure of human IMPase in complex with L690,330 and manganese ions determined at 1.39 Å resolution is reported.

scholarly journals Structural Determination of Functional Units of the Nucleotide Binding Domain (NBD94) of the Reticulocyte Binding Protein Py235 of Plasmodium yoelii

PLoS ONE ◽  
2010 ◽  
Vol 5 (2) ◽  
pp. e9146 ◽  
Author(s):  
Ardina Grüber ◽  
Malathy S. S. Manimekalai ◽  
Asha M. Balakrishna ◽  
Cornelia Hunke ◽  
Jeyaraman Jeyakanthan ◽  
...  
Keyword(s):  
Binding Protein ◽  
Nucleotide Binding ◽  
Plasmodium Yoelii ◽  
Binding Domain ◽  
Structural Determination ◽  
Nucleotide Binding Domain ◽  
Functional Units

A poly(3,4-ethylenedioxythiophene)/carbon nanotube hybrid film for electrocatalytic determination of tertiary butylhydroquinone

The Analyst ◽  
2021 ◽  
Author(s):  
Cunli Wang ◽  
Fudan Zhu ◽  
Zhe Yu ◽  
Xian Zhou ◽  
Wenjing Cheng ◽  
...  
Keyword(s):  
Carbon Nanotube ◽  
Electrochemical Sensor ◽  
Hybrid Film ◽  
Binding Mechanism ◽  
Tertiary Butylhydroquinone ◽  
One Step ◽  
Electrocatalytic Determination

A TBHQ electrochemical sensor was constructed by one-step electrodeposition of a PEDOT–CNT hybrid film. Additionally, the binding mechanism of PEDOT–CNT has also been discussed briefly.

scholarly journals Conformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Smriti Mishra ◽  
Brandy Verhalen ◽  
Richard A Stein ◽  
Po-Chao Wen ◽  
Emad Tajkhorshid ◽  
...  
Keyword(s):  
Atp Hydrolysis ◽  
Conformational Dynamics ◽  
Nucleotide Binding ◽  
Power Stroke ◽  
Spin Labels ◽  
Nucleotide Binding Sites ◽  
Binding Domains ◽  
Cytotoxic Molecules ◽  
Asymmetric Configuration

Multidrug ATP binding cassette (ABC) exporters are ubiquitous ABC transporters that extrude cytotoxic molecules across cell membranes. Despite recent progress in structure determination of these transporters, the conformational motion that transduces the energy of ATP hydrolysis to the work of substrate translocation remains undefined. Here, we have investigated the conformational cycle of BmrCD, a representative of the heterodimer family of ABC exporters that have an intrinsically impaired nucleotide binding site. We measured distances between pairs of spin labels monitoring the movement of the nucleotide binding (NBD) and transmembrane domains (TMD). The results expose previously unobserved structural intermediates of the NBDs arising from asymmetric configuration of catalytically inequivalent nucleotide binding sites. The two-state transition of the TMD, from an inward- to an outward-facing conformation, is driven exclusively by ATP hydrolysis. These findings provide direct evidence of divergence in the mechanism of ABC exporters.

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