English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons93246

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

/persons/resource/persons92166

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

/persons/resource/persons94274

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

/persons/resource/persons93660

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

Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-57FD-9
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 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