1o53

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{{STRUCTURE_1o53| PDB=1o53 | SCENE= }}
{{STRUCTURE_1o53| PDB=1o53 | SCENE= }}
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'''Solution structure of the N-terminal membrane anchor of E. coli enzyme IIA(Glucose)'''
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===Solution structure of the N-terminal membrane anchor of E. coli enzyme IIA(Glucose)===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12717030 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12717030}}
==About this Structure==
==About this Structure==
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1O53 is a [[Single protein]] structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1o0z 1o0z]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O53 OCA].
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1O53 is a [[Single protein]] structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1o0z 1o0z]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O53 OCA].
==Reference==
==Reference==
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[[Category: Wang, G.]]
[[Category: Wang, G.]]
[[Category: Amphipathic helix]]
[[Category: Amphipathic helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:23:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:11:10 2008''

Revision as of 09:11, 29 July 2008

Image:1o53.png

Template:STRUCTURE 1o53

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

Template:ABSTRACT PUBMED 12717030

About this Structure

1O53 is a Single protein structure. This structure supersedes the now removed PDB entry 1o0z. Full experimental information is available from OCA.

Reference

Solution structure of the N-terminal amphitropic domain of Escherichia coli glucose-specific enzyme IIA in membrane-mimetic micelles., Wang G, Keifer PA, Peterkofsky A, Protein Sci. 2003 May;12(5):1087-96. PMID:12717030

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