Signal transduction by the bacterial phosphotransferase system. Diauxie and the crr gene (J. Monod revisited).

Roseman, Saul; Meadow, N D

doi:10.1016/s0021-9258(19)39720-0

Cited by 65 publications

(3 citation statements)

References 11 publications

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“…The molecular basis for the latter regulatory phenomenon is unknown. [For recent reviews, see Meadow et al (1990), Roseman and Meadow (1990), , and Postma and Lengeler (1985). ]…”

mentioning

confidence: 99%

Structural comparison of phosphorylated and unphosphorylated forms of IIIGlc, a signal-transducing protein from Escherichia coli, using three-dimensional NMR techniques

Torchia¹,

Meadow²,

Roseman³

1992

Biochemistry

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The 18.1-kDa protein IIIGlc from Escherichia coli acts as both a phosphocarrier protein in the phosphoenolpyruvate:glycose phosphotransferase system (PTS) and as a signal-transducing protein with respect to the uptake of non-PTS sugars. Phosphorylation of IIIGlc at the N epsilon (N3) position of His-90 was effected through a regeneration system that included MgCl2, DTT, excess PEP, and catalytic amounts of Enzyme I and HPr. NH, 15N, and 13C alpha signal assignments for P-IIIGlc were made through comparison of 15N-1H correlation spectra (HSQC) of uniformly 15N-labeled preparations of phosphorylated and unphosphorylated protein and through analysis of three-dimensional triple-resonance HNCA spectra of P-IIIGlc uniformly labeled with both 15N and 13C. Backbone and side-chain 1H and 13C beta signals were assigned using 3D heteronuclear HCCH-COSY and HCCH-TOCSY spectra of P-IIIGlc. Using this approach, the assignments were made without reference to nuclear Overhauser effect data or assumptions regarding protein structure. The majority of NH, 15N, H alpha, and 13C alpha chemical shifts measured for P-IIIGlc were identical to those obtained for the unphosphorylated protein [Pelton, J. G., Torchia, D. A., Meadow, N. D., Wong, C.-Y., & Roseman, S. (1991) Biochemistry 30, 10043]. Those signals that exhibited shifts corresponded to residues within four segments (1) Leu-87-Gly-100, (2) Val-36-Val-46, (3) His-75-Ser-78, and (4) Ala-131-Val-138. These four segments are in close proximity to the active site residues His-75 and His-90 in the unphosphorylated protein [Worthylake, D., Meadow, N. D., Roseman, S., Liao, D., Hertzberg, O., & Remington, S.J. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 10382], and the chemical shift data provide strong evidence that if any structural changes accompany phosphorylation, they are confined to residues in these four segments. This conclusion is confirmed by comparing NOEs observed in 3D 15N/13C NOESY-HMQC spectra of the two forms of the protein. No NOE differences are seen for residues having the same chemical shifts in IIIGlc and P-IIIGlc. Furthermore, with the exception of residues Ala-76, Asp-94, and Val-96, the NOEs of residues (in the four segments) which exhibited chemical shift differences also had the same NOEs in IIIGlc and P-IIIGlc. In the case of residues Ala-76, Asp-94, and Val-96, minor differences in NOEs, corresponding to interproton distances changes of less than 1.5 A, were observed.(ABSTRACT TRUNCATED AT 400 WORDS)

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“…The molecular basis for the latter regulatory phenomenon is unknown. [For recent reviews, see Meadow et al (1990), Roseman and Meadow (1990), , and Postma and Lengeler (1985). ]…”

mentioning

confidence: 99%

Structural comparison of phosphorylated and unphosphorylated forms of IIIGlc, a signal-transducing protein from Escherichia coli, using three-dimensional NMR techniques

Torchia¹,

Meadow²,

Roseman³

1992

Biochemistry

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“…In addition, glucose is preferred to glycerol, so glycerol kinase must be shut down when glucose is readily available (Zwaig et al, 1970;Holtman et al, 2001). The catalytic activity of GK is controlled through binding to the regulatory protein IIA Glc (Roseman and Meadow, 1990) and fructose 1,6-biphosphate (Zwaig et al, 1970), which are present whenever further phosphorylation of glycerol is not desirable. GK is thought to adopt two distinct conformational states, the open and closed forms.…”

Section: Introductionmentioning

confidence: 99%

Mechanisms of Selectivity in Channels and Enzymes Studied with Interactive Molecular Dynamics

Grayson

Tajkhorshid

Schulten

2003

Biophysical Journal

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Interactive molecular dynamics, a new modeling tool for rapid investigation of the physical mechanisms of biological processes at the atomic level, is applied to study selectivity and regulation of the membrane channel protein GlpF and the enzyme glycerol kinase. These proteins facilitate the first two steps of Escherichia coli glycerol metabolism. Despite their different function and architecture the proteins are found to employ common mechanisms for substrate selectivity: an induced geometrical fit by structurally homologous binding sites and an induced rapid dipole moment reversal. Competition for hydrogen bonding sites with water in both proteins is critical for substrate motion. In glycerol kinase, it is shown that the proposed domain motion prevents competition with water, in turn regulating the binding of glycerol.

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“…Ist allerdings kein PTS-Substrat verfügbar, oder das PEP/Pyruvat-Verhältnis hoch, liegen die Proteine des Phosphotransferasesysteme aufgrund des fehlenden Phosphatakzeptors hauptsächlich phosphoryliert vor (Bettenbrock et al, 2007;Hogema et al, 1998). In diesem Zustand interagiert das EIIA Glc mit der Adenylat Cyclase und aktiviert diese (Park et al, 2006;Roseman and Meadow, 1990). Der aus ATP entstehende second messenger cAMP dient als Ko-Aktivator des CAP (cAMP Bindeprotein).…”

Section: Phosphotransferasesystemeunclassified

Die regulatorischen Funktionen des paralogen Phosphotransferase Systems (PTSNtr) in Escherichia coli.

Lüttmann¹

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Signal transduction by the bacterial phosphotransferase system. Diauxie and the crr gene (J. Monod revisited).

Cited by 65 publications

References 11 publications

Structural comparison of phosphorylated and unphosphorylated forms of IIIGlc, a signal-transducing protein from Escherichia coli, using three-dimensional NMR techniques

Structural comparison of phosphorylated and unphosphorylated forms of IIIGlc, a signal-transducing protein from Escherichia coli, using three-dimensional NMR techniques

Mechanisms of Selectivity in Channels and Enzymes Studied with Interactive Molecular Dynamics

Die regulatorischen Funktionen des paralogen Phosphotransferase Systems (PTSNtr) in Escherichia coli.

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