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1iba

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Revision as of 10:58, 4 August 2021

GLUCOSE PERMEASE (DOMAIN IIB), NMR, 11 STRUCTURES

Structural highlights

1iba is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PTGCB_ECOLI] The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport. This enzyme is also a chemoreceptor monitoring the environment for changes in sugar concentration.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Eberstadt M, Grdadolnik SG, Gemmecker G, Kessler H, Buhr A, Erni B. Solution structure of the IIB domain of the glucose transporter of Escherichia coli. Biochemistry. 1996 Sep 3;35(35):11286-92. PMID:8784182 doi:10.1021/bi960492l

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iba"

@@ Line 3: / Line 3: @@
 <StructureSection load='1iba' size='340' side='right'caption='[[1iba]], [[NMR_Ensembles_of_Models | 11 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1iba]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1iba]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBA FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iba OCA], [http://pdbe.org/1iba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iba RCSB], [http://www.ebi.ac.uk/pdbsum/1iba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iba ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iba OCA], [https://pdbe.org/1iba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iba RCSB], [https://www.ebi.ac.uk/pdbsum/1iba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iba ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PTGCB_ECOLI PTGCB_ECOLI]] The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport. This enzyme is also a chemoreceptor monitoring the environment for changes in sugar concentration.
+[[https://www.uniprot.org/uniprot/PTGCB_ECOLI PTGCB_ECOLI]] The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport. This enzyme is also a chemoreceptor monitoring the environment for changes in sugar concentration.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1iba

From Proteopedia

Revision as of 10:58, 4 August 2021

GLUCOSE PERMEASE (DOMAIN IIB), NMR, 11 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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