Two-dimensional proton NMR studies of histidine-containing protein from Escherichia coli. 1. Sequential resonance assignments
- 18 November 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (23), 7760-7769
- https://doi.org/10.1021/bi00371a071
Abstract
Two-dimensional NMR studies at 500 MHz have been performed on the histidine-containing protein (HPr) from Escherichia coli. HPr is one of the phosphocarrier proteins involved in the bacterial phosphoenolpyruvate:sugar phosphotransferase system that is responsible for the concomitant phosphorylation and translocation of a number of sugars. Sequential resonance assignments of HPr are complete. The conventional method of sequential assignments involving J-correlated spectroscopy (COSY) and nuclear Overhauser spectroscopy (NOESY) has been supplemented by optimized relayed coherence transfer spectroscopy (RELAY) to help overcome the spectral overlap that is inevitable in the spectra of proteins the size of HPr. RELAY experiments were performed in H2O to obtain NH-C.beta.H connectivities and in D2O to obtain C.alpha.H-C.gamma.H connectivities. The abundance of relayed coherence transfer peaks in the two experiments greatly aided in the assignment process of the complicated protein spectrum. The assignments lay the groundwork for the determination of the solution structure of HPr, as described in the accompanying paper [Klevit, R. E., and Waygood, E. B. (1986) Biochemistry)].This publication has 10 references indexed in Scilit:
- Characterization of phosphorylated histidine-containing protein (HPr) of the bacterial phosphoenolpyruvate/sugar phosphotransferase systemBiochemistry, 1985
- Proton NMR studies of .lambda. cro repressor. 1. Selective optimization of two-dimensional relayed coherence transfer spectroscopyBiochemistry, 1985
- Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distancesJournal of Molecular Biology, 1984
- The primary structure of Salmonella typhimurium HPr, a phosphocarrier protein of the phosphoenolpyruvate:glycose phosphotransferase system. A correction.Journal of Biological Chemistry, 1984
- Sugar transport by the bacterial phosphotransferase system. Primary structure and active site of a general phosphocarrier protein (HPr) from Salmonella typhimurium.Journal of Biological Chemistry, 1982
- HPr proteins of different microorganisms studied by proton-high-resolution nuclear magnetic resonance: similarities of structures and mechanismsBiochemistry, 1982
- Preliminary X-ray data for the HPr protein of the phosphoenolpyruvate: Sugar phosphotransferase system of Escherichia coliJournal of Molecular Biology, 1982
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectraJournal of Molecular Biology, 1982
- Enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system of Escherichia coli. Purification to homogeneity and some propertiesCanadian Journal of Biochemistry, 1980
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OHBiopolymers, 1979