1iba
From Proteopedia
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- | [[Image:1iba.gif|left|200px]]<br /> | + | [[Image:1iba.gif|left|200px]]<br /><applet load="1iba" size="450" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1iba" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1iba" /> | caption="1iba" /> | ||
'''GLUCOSE PERMEASE (DOMAIN IIB), NMR, 11 STRUCTURES'''<br /> | '''GLUCOSE PERMEASE (DOMAIN IIB), NMR, 11 STRUCTURES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
- | 1IBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] | + | 1IBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] Known structural/functional Site: <scene name='pdbsite=S1:Phosphorylation Site CYS 35'>S1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IBA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
- | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:33:20 2007'' |
Revision as of 14:23, 18 December 2007
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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
Page seeded by OCA on Tue Dec 18 16:33:20 2007
Categories: Escherichia coli | Protein-N(pi)-phosphohistidine--sugar phosphotransferase | Single protein | Buhr, A. | Eberstadt, M. | Erni, B. | Gemmecker, G. | Grdadolnik, S.G. | Kessler, H. | Inner membrane | Phosphorylation | Phosphotransferase system | Sugar transport | Transferase | Transmembrane