1999
DOI: 10.1007/bf03162178
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Solution structure of the histidine-containing phosphocarrier protein fromStaphylococcus carnosus

Abstract: The solution structure of histidine-containing phosphocarrier protein from Staphylococcus carnosus was determined by two-and three-dimensional nuclear magnetic resonance (NMR) spectroscopy on uniformly 15 N-enriched protein. The main structural element is an antiparallel (3-pleated sheet with four strands A, B, C, and D arranged with the topology A-D-B-C. Strand A comprises residues 2 to 8, strand B residues 32 to 37, strand C reidues 40 to 43, and strand D residues 59 to 66. Three right-handed helices are arr… Show more

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Cited by 11 publications
(30 citation statements)
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References 54 publications
(55 reference statements)
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“…As described earlier (28), for the HPr protein of S. aureus there is an interesting exception: the cross peaks between the H ␥ proton of the hydroxyl group and the H ␣ and H ␤ protons of Ser31 can be observed directly in the TOCSY spectra at 303 K. This is a typical spectroscopic feature of HPr proteins which has been described for HPr from Staphylococcus carnosus (14) as well as HPr from E. coli (20), which both contain a conserved serine residue at this position. The hydroxyl proton resonances of Ser31 could be observed at 5.58 ppm in HPr from S. carnosus and at 5.77 ppm in HPr from E. coli, very close to the resonance position of 5.56 ppm obtained for HPr from S. aureus.…”
Section: Resultssupporting
confidence: 54%
“…As described earlier (28), for the HPr protein of S. aureus there is an interesting exception: the cross peaks between the H ␥ proton of the hydroxyl group and the H ␣ and H ␤ protons of Ser31 can be observed directly in the TOCSY spectra at 303 K. This is a typical spectroscopic feature of HPr proteins which has been described for HPr from Staphylococcus carnosus (14) as well as HPr from E. coli (20), which both contain a conserved serine residue at this position. The hydroxyl proton resonances of Ser31 could be observed at 5.58 ppm in HPr from S. carnosus and at 5.77 ppm in HPr from E. coli, very close to the resonance position of 5.56 ppm obtained for HPr from S. aureus.…”
Section: Resultssupporting
confidence: 54%
“…4 The MD and molecular mechanics calculation were performed with the parm98 parameter set 25 and the TIP3P model for water. 26 The program AMBER 6.0 27 was used for the simulations performed with the Berendsen thermostat, and the program ORAC 4.0 28 for the simulations performed with the NoseHoover thermostat.…”
Section: Methodsmentioning
confidence: 99%
“…The RMSD values of atomic coordinates between the mean conformers are in the ranges of 0.68 -1.0 Å for all atoms and of 0.57-0.95 Å for heavy atoms: this is of the same order of value as the RMSD values between the conformers of the NMR structure. 4 The global changes induced on the protein structure by the hydrostatic pressure are on average of similar amplitude than the conformational variability in the NMR structure determined at 0.1 MPa. Mean RMSD values of 0.50, 0.64, and 0.63 Å are found for the 2-7, 20 -41, and 50 -84 regions, which are the best defined regions in the NMR structure.…”
Section: Global Changes Induced By Pressurementioning
confidence: 99%
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