1O53

Solution structure of the N-terminal membrane anchor of E. coli enzyme IIA(Glucose)

Replaces:  1O0Z

Summary for 1O53

• Entry DOI: 10.2210/pdb1o53/pdb
• Related: 1GGR 2F3G
• NMR Information: BMRB: 5708
• Descriptor: PTS system, glucose-specific IIA component (1 entity in total)
• Functional Keywords: amphipathic helix, transferase
• Cellular location: Cytoplasm: P08837
• Total number of polymer chains: 1
• Total formula weight: 1696.98

Authors

Wang, G.,Keifer, P.A.,Peterkofsky, A. (deposition date: 2003-08-11, release date: 2003-08-19, Last modification date: 2023-12-27)

Primary citation

Wang, G.,Keifer, P.A.,Peterkofsky, A.
Solution structure of the N-terminal amphitropic domain of Escherichia coli glucose-specific enzyme IIA in membrane-mimetic micelles
Protein Sci., 12:1087-1096, 2003

PubMed Abstract: The N-terminal domain of enzyme IIA(Glc) of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system confers amphitropism to the protein, allowing IIA(Glc) to shuttle between the cytoplasm and the membrane. To further understand this amphitropic protein, we have elucidated, by NMR spectroscopy, the solution structure of a synthetic peptide corresponding to the N-terminal domain of IIA(Glc). In water, this peptide is predominantly disordered, consistent with previous data obtained in the absence of membranes. In detergent micelles of dihexanoylphosphatidylglycerol (DHPG) or sodium dodecylsulfate (SDS), however, residues Phe 3-Val 10 of the peptide adopt a helical conformation in the ensemble of structures calculated on the basis of NOE-derived distance restraints. The root mean square deviations for superimposing the backbone atoms of the helical region are 0.18 A in DHPG and 0.22 A in SDS. The structure, chemical shifts, and spin-spin coupling constants all indicate that, of the four lysines in the N-terminal domain of IIA(Glc), only Lys 5 and Lys 7 in the amphipathic helical region interact with DHPG. In addition, the peptide-detergent interactions were investigated using intermolecular NOESY experiments. The aliphatic chains of anionic detergents DHPG, SDS, and 2,2-dimethyl-2-silapentane-5-sulfonate sodium salt (DSS) all showed intermolecular NOE cross-peaks to the peptide, providing direct evidence for the putative membrane anchor of IIA(Glc) in binding to the membrane-mimicking micelles.

PubMed: 12717030
DOI: 10.1110/ps.0301503

Experimental method

SOLUTION NMR