1iba

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==Overview==
==Overview==
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The structure of the IIBGlc domain of the Escherichia coli transporter for, glucose was determined by multidimensional heteronuclear NMR. The glucose, transporter (IICBGlc) belongs to the bacterial phosphotransferase system., It mediates uptake with concomittant phosphorylation of glucose. The, N-terminal IICGlc domain spans the membrane, the C-terminal IIBGlc domain, (residues 386-477) contains the phosphorylation site, Cys421. The, structure of the subclonal IIB domain was determined based on 927, conformational constraints, including 744 NOE derived upper bounds, 43, constraints of ranges of dihedral angles based on measurements of vicinal, coupling constants, and 70 upper and lower bound constraints associated, with 35 hydrogen bonds. The distance geometry interpretation of the NMR, data is based on the previously published sequence-specific 1H, 15N, and, 13C resonance assignments [Golic Grdadolnik et al. (1994) Eur. J. Biochem., 219, 945-952]. The sequence of the secondary structure elements of IIB is, alpha 1 beta 1 beta 2 alpha 2 beta 3 beta 4 alpha 3. The basic fold, consists of a split alpha/beta-sandwich composed of an antiparallel sheet, with strand order beta 1 beta 2 beta 4 beta 3 and three alpha-helices, superimposed onto one side of the sheet. The hydrophobic helix alpha 1 is, packed against helices alpha 2, alpha 3, and the beta-sheet. The, phosphorylation site (Cys421) is at the end of beta 1 on the, solvent-exposed face of the sheet surrounded by Asp419, Thr423 Arg424, Arg426, and Gln456 which are invariant in 15 homologous IIB domains from, other PTS transporters.
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The structure of the IIBGlc domain of the Escherichia coli transporter for glucose was determined by multidimensional heteronuclear NMR. The glucose transporter (IICBGlc) belongs to the bacterial phosphotransferase system. It mediates uptake with concomittant phosphorylation of glucose. The N-terminal IICGlc domain spans the membrane, the C-terminal IIBGlc domain (residues 386-477) contains the phosphorylation site, Cys421. The structure of the subclonal IIB domain was determined based on 927 conformational constraints, including 744 NOE derived upper bounds, 43 constraints of ranges of dihedral angles based on measurements of vicinal coupling constants, and 70 upper and lower bound constraints associated with 35 hydrogen bonds. The distance geometry interpretation of the NMR data is based on the previously published sequence-specific 1H, 15N, and 13C resonance assignments [Golic Grdadolnik et al. (1994) Eur. J. Biochem. 219, 945-952]. The sequence of the secondary structure elements of IIB is alpha 1 beta 1 beta 2 alpha 2 beta 3 beta 4 alpha 3. The basic fold consists of a split alpha/beta-sandwich composed of an antiparallel sheet with strand order beta 1 beta 2 beta 4 beta 3 and three alpha-helices superimposed onto one side of the sheet. The hydrophobic helix alpha 1 is packed against helices alpha 2, alpha 3, and the beta-sheet. The phosphorylation site (Cys421) is at the end of beta 1 on the solvent-exposed face of the sheet surrounded by Asp419, Thr423 Arg424, Arg426, and Gln456 which are invariant in 15 homologous IIB domains from other PTS transporters.
==About this Structure==
==About this Structure==
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[[Category: Erni, B.]]
[[Category: Erni, B.]]
[[Category: Gemmecker, G.]]
[[Category: Gemmecker, G.]]
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[[Category: Grdadolnik, S.G.]]
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[[Category: Grdadolnik, S G.]]
[[Category: Kessler, H.]]
[[Category: Kessler, H.]]
[[Category: inner membrane]]
[[Category: inner membrane]]
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:01 2008''

Revision as of 11:10, 21 February 2008


1iba

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GLUCOSE PERMEASE (DOMAIN IIB), NMR, 11 STRUCTURES

Overview

The structure of the IIBGlc domain of the Escherichia coli transporter for glucose was determined by multidimensional heteronuclear NMR. The glucose transporter (IICBGlc) belongs to the bacterial phosphotransferase system. It mediates uptake with concomittant phosphorylation of glucose. The N-terminal IICGlc domain spans the membrane, the C-terminal IIBGlc domain (residues 386-477) contains the phosphorylation site, Cys421. The structure of the subclonal IIB domain was determined based on 927 conformational constraints, including 744 NOE derived upper bounds, 43 constraints of ranges of dihedral angles based on measurements of vicinal coupling constants, and 70 upper and lower bound constraints associated with 35 hydrogen bonds. The distance geometry interpretation of the NMR data is based on the previously published sequence-specific 1H, 15N, and 13C resonance assignments [Golic Grdadolnik et al. (1994) Eur. J. Biochem. 219, 945-952]. The sequence of the secondary structure elements of IIB is alpha 1 beta 1 beta 2 alpha 2 beta 3 beta 4 alpha 3. The basic fold consists of a split alpha/beta-sandwich composed of an antiparallel sheet with strand order beta 1 beta 2 beta 4 beta 3 and three alpha-helices superimposed onto one side of the sheet. The hydrophobic helix alpha 1 is packed against helices alpha 2, alpha 3, and the beta-sheet. The phosphorylation site (Cys421) is at the end of beta 1 on the solvent-exposed face of the sheet surrounded by Asp419, Thr423 Arg424, Arg426, and Gln456 which are invariant in 15 homologous IIB domains from other PTS transporters.

About this Structure

1IBA is a Single protein structure of sequence from Escherichia coli. Active as Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Solution structure of the IIB domain of the glucose transporter of Escherichia coli., Eberstadt M, Grdadolnik SG, Gemmecker G, Kessler H, Buhr A, Erni B, Biochemistry. 1996 Sep 3;35(35):11286-92. PMID:8784182

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