PMID:9074635: Difference between revisions

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<span style = 'font-size: large'> '''Gschwind, RM, Gemmecker, G, Leutner, M, Kessler, H, Gutknecht, R, Lanz, R, Flükiger, K and Erni, B'''  (1997) Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures.''FEBS Lett.'' '''404''':45-50</span>
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!align=left  |Citation
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'''Gschwind, RM, Gemmecker, G, Leutner, M, Kessler, H, Gutknecht, R, Lanz, R, Flükiger, K and Erni, B'''  (1997) Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures. ''FEBS Lett.'' '''404''':45-50
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!align=left  |Abstract
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The mannose transporter of the Escherichia coli bacterial phosphotransferase system consists of three subunits: IIAB, IIC and IID. IIABMan transfers phosphoryl groups to the transported substrate via phosphohistidine intermediates. Its IIB domain was overexpressed and isotopically labelled with 13C, 15N and 2H. Heteronuclear 3D triple-resonance NMR experiments combined with a semi-automatic assignment procedure yielded the sequential assignment of the 1H, 13C and 15N backbone resonances. Based on the evaluation of conformationally sensitive parameters, the secondary structure of the IIBMan domain has been determined as an alpha/beta twisted open-sheet structure consisting of a six-stranded parallel beta-sheet with the novel strand order 3-2-4-1-5-6, six helices and a short two-stranded antiparallel beta-sheet.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9074635 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || The mannose transporter of the Escherichia coli bacterial phosphotransferase system consists of three subunits: IIAB, IIC and IID. IIABMan transfers phosphoryl groups to the transported substrate via phosphohistidine intermediates. Its IIB domain was overexpressed and isotopically labelled with 13C, 15N and 2H. Heteronuclear 3D triple-resonance NMR experiments combined with a semi-automatic assignment procedure yielded the sequential assignment of the 1H, 13C and 15N backbone resonances. Based on the evaluation of conformationally sensitive parameters, the secondary structure of the IIBMan domain has been determined as an alpha/beta twisted open-sheet structure consisting of a six-stranded parallel beta-sheet with the novel strand order 3-2-4-1-5-6, six helices and a short two-stranded antiparallel beta-sheet.
!align=left  |Keywords
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Amino Acid Sequence; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli/metabolism; Magnetic Resonance Spectroscopy; Mannose/metabolism; Molecular Sequence Data; Monosaccharide Transport Proteins/chemistry; Monosaccharide Transport Proteins/metabolism; Phosphoenolpyruvate Sugar Phosphotransferase System/chemistry; Phosphoenolpyruvate Sugar Phosphotransferase System/metabolism; Protein Folding; Protein Structure, Secondary; Structure-Activity Relationship
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9074635 PubMed]
 
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Latest revision as of 04:56, 15 September 2013

Citation

Gschwind, RM, Gemmecker, G, Leutner, M, Kessler, H, Gutknecht, R, Lanz, R, Flükiger, K and Erni, B (1997) Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures. FEBS Lett. 404:45-50

Abstract

The mannose transporter of the Escherichia coli bacterial phosphotransferase system consists of three subunits: IIAB, IIC and IID. IIABMan transfers phosphoryl groups to the transported substrate via phosphohistidine intermediates. Its IIB domain was overexpressed and isotopically labelled with 13C, 15N and 2H. Heteronuclear 3D triple-resonance NMR experiments combined with a semi-automatic assignment procedure yielded the sequential assignment of the 1H, 13C and 15N backbone resonances. Based on the evaluation of conformationally sensitive parameters, the secondary structure of the IIBMan domain has been determined as an alpha/beta twisted open-sheet structure consisting of a six-stranded parallel beta-sheet with the novel strand order 3-2-4-1-5-6, six helices and a short two-stranded antiparallel beta-sheet.

Links

PubMed

Keywords

Amino Acid Sequence; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli/metabolism; Magnetic Resonance Spectroscopy; Mannose/metabolism; Molecular Sequence Data; Monosaccharide Transport Proteins/chemistry; Monosaccharide Transport Proteins/metabolism; Phosphoenolpyruvate Sugar Phosphotransferase System/chemistry; Phosphoenolpyruvate Sugar Phosphotransferase System/metabolism; Protein Folding; Protein Structure, Secondary; Structure-Activity Relationship

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