Goerler, A. and Hengstenberg, W. and Kravanja, M. and Beneicke, W. and Maurer, T. and Kalbitzer, Hans Robert (1999) Solution structure of the histidine-containing phosphocarrier protein from Staphylococcus carnosus. APPLIED MAGNETIC RESONANCE, 17 (2-3). pp. 465-480. ISSN 0937-9347,
Full text not available from this repository. (Request a copy)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 beta-pleated sheet with four strands At 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 53. Strands B and C of the beta-pleated sheet are connected by a type II' turn. The hydroxyl proton of Ser-31 is exchanging 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 N(delta 1) atom of His-15, accepting the phosphoryl from enzyme I, is exposed to the solvent.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | DEPENDENT PHOSPHOTRANSFERASE SYSTEM; 2-DIMENSIONAL NMR-SPECTROSCOPY; NUCLEAR-MAGNETIC-RESONANCE; ESCHERICHIA-COLI; BACILLUS-SUBTILIS; SUGAR-TRANSPORT; RESOLUTION STRUCTURE; TERTIARY STRUCTURE; HPR; PHOSPHOENOLPYRUVATE; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 29 Nov 2022 09:30 |
| Last Modified: | 29 Nov 2022 09:30 |
| URI: | https://pred.uni-regensburg.de/id/eprint/48608 |
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