scholarly journals The Crystal Structure of Beryllofluoride Spo0F in Complex with the Phosphotransferase Spo0B Represents a Phosphotransfer Pretransition State

2006 ◽  
Vol 188 (13) ◽  
pp. 4970-4977 ◽  
Author(s):  
Kottayil I. Varughese ◽  
Igor Tsigelny ◽  
Haiyan Zhao
Keyword(s):  
Crystal Structure ◽  
Bacillus Subtilis ◽  
Transition State ◽  
Histidine Kinase ◽  
In Silico ◽  
Phosphoryl Group ◽  
Phosphoryl Transfer ◽  
Regulatory Circuits ◽  
Phosphoryl Groups ◽  
In Silico Models

ABSTRACT A number of regulatory circuits in biological systems function through the exchange of phosphoryl groups from one protein to another. Spo0F and Spo0B are components of a phosphorelay that control sporulation in the bacterium Bacillus subtilis through the exchange of a phosphoryl group. Using beryllofluoride as a mimic for phosphorylation, we trapped the interaction of the phosphorylated Spo0F with Spo0B in the crystal lattice. The transition state of phosphoryl transfer continues to be a highly debated issue, as to whether it is associative or dissociative in nature. The geometry of Spo0F binding to Spo0B favors an associative mechanism for phosphoryl transfer. In order to visualize the autophosphorylation of the histidine kinase, KinA, and the subsequent phosphoryl transfer to Spo0F, we generated in silico models representing these reaction steps.

scholarly journals Insight into the sporulation phosphorelay: Crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD

2013 ◽  
Vol 22 (5) ◽  
pp. 564-576 ◽  
Author(s):  
R. Wu ◽  
M. Gu ◽  
R. Wilton ◽  
G. Babnigg ◽  
Y. Kim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Bacillus Subtilis ◽  
Histidine Kinase ◽  
Insight Into

scholarly journals The Crystal Structure of Bacillus subtilis YycI Reveals a Common Fold for Two Members of an Unusual Class of Sensor Histidine Kinase Regulatory Proteins

2007 ◽  
Vol 189 (8) ◽  
pp. 3290-3295 ◽  
Author(s):  
Eugenio Santelli ◽  
Robert C. Liddington ◽  
Michael A. Mohan ◽  
James A. Hoch ◽  
Hendrik Szurmant
Keyword(s):  
Crystal Structure ◽  
Bacillus Subtilis ◽  
Sequence Homology ◽  
Histidine Kinase ◽  
Direct Interaction ◽  
Regulatory Proteins ◽  
Sensor Histidine Kinase ◽  
Periplasmic Proteins ◽  
Terminal Domains

ABSTRACT YycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-Å resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite nearly undetectable sequence homology (10%) between the two proteins.

Memapsin 2, a drug target for Alzheimer's disease

2003 ◽  
Vol 70 ◽  
pp. 213-220 ◽  
Author(s):  
Gerald Koelsch ◽  
Robert T. Turner ◽  
Lin Hong ◽  
Arun K. Ghosh ◽  
Jordan Tang
Keyword(s):  
Crystal Structure ◽  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Transition State ◽  
Amyloid Precursor Protein ◽  
Therapeutic Target ◽  
Drug Target ◽  
Aspartic Protease ◽  
Precursor Protein ◽  
Memapsin 2

Mempasin 2, a ϐ-secretase, is the membrane-anchored aspartic protease that initiates the cleavage of amyloid precursor protein leading to the production of ϐ-amyloid and the onset of Alzheimer's disease. Thus memapsin 2 is a major therapeutic target for the development of inhibitor drugs for the disease. Many biochemical tools, such as the specificity and crystal structure, have been established and have led to the design of potent and relatively small transition-state inhibitors. Although developing a clinically viable mempasin 2 inhibitor remains challenging, progress to date renders hope that memapsin 2 inhibitors may ultimately be useful for therapeutic reduction of ϐ-amyloid.

scholarly journals Safety Assessment of Bacillus subtilis MB40 for Use in Foods and Dietary Supplements

Nutrients ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 733
Author(s):  
Jessica L. Spears ◽  
Richard Kramer ◽  
Andrey I. Nikiforov ◽  
Marisa O. Rihner ◽  
Elizabeth A. Lambert
Keyword(s):  
Antibiotic Resistance ◽  
Bacillus Subtilis ◽  
Dietary Supplements ◽  
Genome Sequencing ◽  
In Silico ◽  
Safety Assessment ◽  
In Vivo Studies ◽  
Strain Identification ◽  
Consumer Safety

With the growing popularity of probiotics in dietary supplements, foods, and beverages, it is important to substantiate not only the health benefits and efficacy of unique strains but also safety. In the interest of consumer safety and product transparency, strain identification should include whole-genome sequencing and safety assessment should include genotypic and phenotypic studies. Bacillus subtilis MB40, a unique strain marketed for use in dietary supplements, and food and beverage, was assessed for safety and tolerability across in silico, in vitro, and in vivo studies. MB40 was assessed for the absence of undesirable genetic elements encoding toxins and mobile antibiotic resistance. Tolerability was assessed in both rats and healthy human volunteers. In silico and in vitro testing confirmed the absence of enterotoxin and mobile antibiotic resistance genes of safety concern to humans. In rats, the no-observed-adverse-effect level (NOAEL) for MB40 after repeated oral administration for 14 days was determined to be 2000 mg/kg bw/day (equivalent to 3.7 × 1011 CFU/kg bw/day). In a 28 day human tolerability trial, 10 × 109 CFU/day of MB40 was well tolerated. Based on genome sequencing, strain characterization, screening for undesirable attributes and evidence of safety by appropriately designed safety evaluation studies in rats and humans, Bacillus subtilis MB40 does not pose any human health concerns under the conditions tested.

Crystal Structure of Urate Oxidase from Bacillus Subtilis 168

2019 ◽  
Vol 64 (7) ◽  
pp. 1126-1133 ◽  
Author(s):  
A. Nayab ◽  
S. A. Moududee ◽  
Y. Shi ◽  
Y. Jiang ◽  
Q. Gong
Keyword(s):  
Crystal Structure ◽  
Bacillus Subtilis ◽  
Urate Oxidase ◽  
Bacillus Subtilis 168
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