Solution structure of the 40,000 M(r) phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr

Nature Structural Biology

Volumn 6, Issue 2, 1999, Pages 166-173

  Garrett, Daniel S ^a   Seok, Yeong Jae ^b,c   Peterkofsky, Alan ^b   Gronenborn, Angela M ^a   Marius Clore, G ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^c Seoul National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; PHOSPHOENOLPYRUVATE; PHOSPHOTRANSFERASE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEX FORMATION; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE SYSTEM; PHOSPHOTRANSFERASES (NITROGENOUS GROUP ACCEPTOR); PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS;

EID: 0032939176     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/5854     Document Type: Article

References (12)

1. Postma, P.W., Lengeler, J.W. & Jacobson, G.R. Phosphoenolpyruvate:carbohydrate phosphotransferase systems. In Echerchia coli and Salmonella: Cellular and Molecular Biology (ed. Neidhardt F.C.) 1149-1174 (ASM Press, Washington DC; 1996).
2. Herzberg, O & Klevit R. Unraveling a bacterial hexose transport pathway. Curr. Opin. Struct. Biol. 4, 814-822 (1994).
3. Licalsi, C., Crocenzi, T.S., Freire, E. & Roseman, S. Sugar transport by the bacterial phosphotransferase system: structural and thermodynamic domains of Enzyme I of Salmonella typhimurium. J. Biol. Chem. 266, 19519-19527 (1991).
4. Lee, B.R., Lecchi, P., Pannell, L., Jaffe, H. & Peterkofsky, A. Identification of the N-terminal domain of Enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransfease system produced by proteolytic digestion. Arch. Biochem. Biophys. 312, 121-124 (1994).
5. Seok, Y.-J., Lee, B.R., Zhu, P.-P. & Peterkofsky, A. Importance of the carboxyl terminal domain of Enzyme I of the Escnerichia coli phosphoenolpyruvate:sugar phosphotransferase system for phosphoryl donor specificity. Proc. Natl. Acad. Sci. USA 93, 347-351 (1996).
6. Chauvin, F., Fomenkov, A., Johnson, C.R. & Roseman, S. The N-terminal domain of Echerichia coli enzyme I of the phosphoenolpyruvate/glycose phosphotransferase system: molecular cloning and characterization. Proc. Natl. Acad. Sci. USA 93, 7028-7031 (1996).
7. Liao, D.-I. et al. The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E coli PEP:sugar phosphotransferase system and a model of the phosphotransfer complex with HPr. Structure 4, 861-872 (1996).
8. Garrett, D.S. et al. Solution structure of the 30 kDa N-terminal domain of Enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Biochemistry 36, 2517-2530 (1997).
9. Wittekind, M. et al. Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy. Prot. Sci. 1, 1363-1376 (1992).
10. Herzberg, O. et al. Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0 ̊ resolution. Proc. Natl. Acad. Sci. USA 89, 2499-2503 (1992).
11. Kalbitzer, H.R. & Henstenberg, W. The solution structure of the histidine-containing protein (HPr) from Staphylococcus aureus as determined by two-dimensional 1H-NMR spectroscopy. Eur. J. Biochem. 216, 205-214 (1993).
12. Jia, Z., Quail, J.W., Waygood, E.B. & Delbaere, L.T. The 2.0 ̊ resolution structure of the Escherichia coli histidine-containing phosphocarrier protein HPr: a redetermination. J. Biol. Chem. 268, 22490-22501 (1993).