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Solution structure of the histidine-containing phosphocarrier protein from Staphylococcus carnosus

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons93246

Görler,  Adrian
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons92166

Beneicke,  Wolfgang
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons94274

Maurer,  Till
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons93660

Kalbitzer,  Hans Robert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Görler, A., Hengstenberg, W., Kravanja, M., Beneicke, W., Maurer, T., & Kalbitzer, H. R. (1999). Solution structure of the histidine-containing phosphocarrier protein from Staphylococcus carnosus. Applied Magnetic Resonance, 17(2), 465-480. Retrieved from http://link.springer.com/article/10.1007/BF03162178.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0024-57FD-9
Zusammenfassung
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 15N-enriched protein. The main structural element is an antiparallel beta-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 arranged on top of the beta-pleated sheet. Helix a reaches from residue 16 to 29, helix b from residue 48 to 53, and helix c from residue 72 to 83. Strands B and C of the beta-pleated sheet are connected by a type II turn. The hydroxyl proton of Ser-31 is ex-changing with the solvent so slowly that cross peaks can be detected in two-dimensional NMR spectra based on homonuclear J-couplings. The imidazole ring of the active-center His-15, which is partly charged in the structure determined at pH 7.2, is located above the N-terminal end of helix a, perpendicular to its axis. The Nδ1 atom of His-15, accepting the phosphoryl from enzyme I, is exposed to the solvent