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Title: Structure and Function of the Genomically Encoded Fosfomycin Resistance Enzyme, FosB, from Staphylococcus aureus

Authors:
; ; ; ; ; ; ; ;  [1];  [2];  [2]
  1. Vanderbilt
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1121472
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemistry; Journal Volume: 53; Journal Issue: (4) ; 02, 2014
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Thompson, Matthew K., Keithly, Mary E., Goodman, Michael C., Hammer, Neal D., Cook, Paul D., Jagessar, Kevin L., Harp, Joel, Skaar, Eric P., Armstrong, Richard N., Grand Valley), and Vanderbilt-MED). Structure and Function of the Genomically Encoded Fosfomycin Resistance Enzyme, FosB, from Staphylococcus aureus. United States: N. p., 2014. Web. doi:10.1021/bi4015852.
Thompson, Matthew K., Keithly, Mary E., Goodman, Michael C., Hammer, Neal D., Cook, Paul D., Jagessar, Kevin L., Harp, Joel, Skaar, Eric P., Armstrong, Richard N., Grand Valley), & Vanderbilt-MED). Structure and Function of the Genomically Encoded Fosfomycin Resistance Enzyme, FosB, from Staphylococcus aureus. United States. doi:10.1021/bi4015852.
Thompson, Matthew K., Keithly, Mary E., Goodman, Michael C., Hammer, Neal D., Cook, Paul D., Jagessar, Kevin L., Harp, Joel, Skaar, Eric P., Armstrong, Richard N., Grand Valley), and Vanderbilt-MED). Mon . "Structure and Function of the Genomically Encoded Fosfomycin Resistance Enzyme, FosB, from Staphylococcus aureus". United States. doi:10.1021/bi4015852.
@article{osti_1121472,
title = {Structure and Function of the Genomically Encoded Fosfomycin Resistance Enzyme, FosB, from Staphylococcus aureus},
author = {Thompson, Matthew K. and Keithly, Mary E. and Goodman, Michael C. and Hammer, Neal D. and Cook, Paul D. and Jagessar, Kevin L. and Harp, Joel and Skaar, Eric P. and Armstrong, Richard N. and Grand Valley) and Vanderbilt-MED)},
abstractNote = {},
doi = {10.1021/bi4015852},
journal = {Biochemistry},
number = (4) ; 02, 2014,
volume = 53,
place = {United States},
year = {Mon Aug 25 00:00:00 EDT 2014},
month = {Mon Aug 25 00:00:00 EDT 2014}
}
  • V8 protease, an extracellular protease of Staphylococcus aureus, is related to the pancreatic serine proteases. The enzyme cleaves peptide bonds exclusively on the carbonyl side of aspartate and glutamate residues. Unlike the pancreatic serine proteases, V8 protease possesses no disulfide bridges. This is a major evolutionary difference, as all pancreatic proteases have at least two disulfide bridges. The structure of V8 protease shows structural similarity with several other serine proteases, specifically the epidermolytic toxins A and B from S. aureus and trypsin, in which the conformation of the active site is almost identical. V8 protease is also unique in thatmore » the positively charged N-terminus is involved in determining the substrate-specificity of the enzyme.« less
  • Enzyme III/sup mtl/ is part of the mannitol phosphotransferase system of Staphylococcus aureus and Staphylococcus carnosus and is phosphorylated by phosphoenolpyruvate in a reaction sequence requiring enzyme I (phosphoenolpyruvate-protein phosphotransferase) and the histidine-containing protein HPr. In this paper, the authors report the isolation of III/sup mtl/ from both S. aureus and S. carnosus and the characterization of the active center. After phosphorylation of III/sup mtl/ with (/sup 32/P)PEP, enzyme I, and HPr, the phosphorylated protein was cleaved with endoproteinase GLu(C). The amino acid sequence of the S. aureus peptide carrying the phosphoryl group was found to be Gln-Val-Val-Ser-Thr-Phe-Met-Gly-Asn-Gly-Leu-Ala-Ile-Pro-His-Gly-Thr-Asp-Asp. The correspondingmore » peptide from S. carnosus shows an equal sequence except that the first residue is Ala instead of Gln. These peptides both contain a single histidyl residue which they assume to carry the phosphoryl group. All proteins of the PTS so far investigated indeed carry the phosphoryl group attached to a histidyl residue. According to sodium dodecyl sulfate gels, the molecular weight of the III/sup mtl/ proteins was found to be 15,000. They have also determined the N-terminal sequence of both proteins. Comparison of the III/sup mtl/ peptide sequences and the C-terminal part of the enzyme II/sup mtl/ of Escherichia coli reveals considerable sequence homology, which supports the suggestion that II/sup mtl/ of E. coli is a fusion protein of a soluble III protein with a membrane-bound enzyme II.« less
  • The radiation resistance of bacterial suspensions and the effects of amidine solutions on radiation resistance were investigated. Radiation effects were determined by counting the number of surviving cells and thsir ability to colonize. B. anthracis, B. cereus, Cand. albicans, and Staph. aureus-209 were used in the studies. The B anthracis and B. cereus showed high resistance to radirtion to 300 r; neither of the microorganisms vary their radiosensitivity in the presence of amidine compounds. The suapension of Cand. albicans (at a gamma dose of 50 kr) showed good radioresistance. The data indicate that the best radioprotection achieved with amidine solutionsmore » was from 1: 500 to I: 2500; with stronger solutions the survival drops and at 1:4000 there was no protection. In Staphylococcus aureus, amidines exMbited radioprotective properties in the form of a sensitizer. The radioinduced damage with alpha TA begins with solution of 1: 3000 and disappears at about 1: 30,000. lt is postulated that radiosensitizrtion properties of alpha FA in Staph. aureus are the result of its sprtial relation to the furan ring and to its grouping. (R.V.J.)« less
  • Of 113 lactobacilli isolated from radurized (5 kGy) minced meat, 7 Lactobacillus sake strains, 1 L. curvatus strain, and 1 L. farciminis strain were used for radiation resistance studies in a semisynthetic substrate (i.e., modified MRS broth). Five reference Lactobacillus spp. one Staphylococcus aureus strain, and one Salmonella typhimurium strain were used for comparative purposes. All L. sake isolates exhibited the phenomenon of being more resistant to gamma-irradiation in the exponential (log) phase than in the stationary phase of their growth cycles by a factor of 28%. Four reference strains also exhibited this phenomenon, with L. sake (DSM 20017) showingmore » a 68% increase in resistance in the log phase over the stationary phase. This phenomenon was not common to all bacteria tested and is not common to all strains with high radiation resistance. Four L. sake isolates and three reference strains were used in radiation sensitivity testing in a natural food system (i.e., meat). The bacteria were irradiated in minced meat and packaged under four different conditions (air, vacuum, CO/sub 2/, and N/sub 2/). Organisms exhibited the highest death rate (lowest D/sub 10/ values (doses required to reduce the logarithm of the bacterial population by 1) under CO/sub 2/ packaging conditions, but resistance to irradiation was increased under N/sub 2/. The D/sup 10/ values of the isolates were generally greater than those of the reference strains. The D/sup 10/ values were also higher (approximately two times) in meat than in a semisynthetic growth medium.« less